Coagulation factor XI

Structure name

factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes

Structure deposition date

2021-12-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Coagulation factor XI

Peptide B name

Coagulation factor XI

Peptide A accession

Peptide B accession

Peptide A residue number

339

Peptide B residue number

339

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Coagulation factor XI at cysteines 500 and 380 (122 and 362 respectively in this structure).

Details

Redox score ?

PDB code

5qtx

Structure name

factor xia in complex with the inhibitor ethyl (2r,7s)-7-({(2e)-3-[5- chloro-2-(1h-tetrazol-1-yl)phenyl]prop-2-enoyl}amino)-14- [(methoxycarbonyl)amino]-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9- benzodiazacyclotridecine-2-carboxylate

Structure deposition date

2019-11-13

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Coagulation factor XI

Peptide B name

Coagulation factor XI

Peptide A accession

Peptide B accession

Peptide A residue number

500

Peptide B residue number

380

Ligandability

Cysteine 500 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 380 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 432 of Coagulation factor XI and cysteine 107 of Ecotin (58 and 87 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

1xxd

Structure name

crystal structure of the fxia catalytic domain in complex with mutated ecotin

Structure deposition date

2004-11-04

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Coagulation factor XI

Peptide B name

Ecotin

Peptide A accession

Peptide B accession

P23827

Peptide A residue number

432

Peptide B residue number

107

Ligandability

Cysteine 432 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 107 of Ecotin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 432 of Coagulation factor XI and cysteine 300 of Amyloid-beta precursor protein (58 and 14 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

1zjd

Structure name

crystal structure of the catalytic domain of coagulation factor xi in complex with kunitz protease inhibitor domain of protease nexin ii

Structure deposition date

2005-04-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Coagulation factor XI

Peptide B name

Amyloid-beta precursor protein

Peptide A accession

Peptide B accession

P05067

Peptide A residue number

432

Peptide B residue number

300

Ligandability

Cysteine 432 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 300 of Amyloid-beta precursor protein

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 416 of Coagulation factor XI and cysteine 70 of Ecotin (40 and 50 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

1xx9

Structure name

crystal structure of the fxia catalytic domain in complex with ecotinm84r

Structure deposition date

2004-11-04

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Coagulation factor XI

Peptide B name

Ecotin

Peptide A accession

Peptide B accession

P23827

Peptide A residue number

416

Peptide B residue number

Ligandability

Cysteine 416 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 70 of Ecotin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 20 and 103 (2 and 85 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

human recombinant coagulation fxi in complex with a peptide derived from human high molecular weight kininogen (hkp)

Structure deposition date

2016-02-08

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

Residue number B

103

Peptide name

Coagulation factor XI

Ligandability

Cysteine 20 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 103 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 571 and 599 (553 and 581 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

human recombinant coagulation fxi in complex with a peptide derived from human high molecular weight kininogen (hkp)

Structure deposition date

2016-02-08

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

% buried

Peptide accession

Residue number A

571

Residue number B

599

Peptide name

Coagulation factor XI

Ligandability

Cysteine 571 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 599 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 514 and 581 (136 and 201 respectively in this structure).

Details

Redox score ?

PDB code

5q0g

Structure name

factor xia in complex with the inhibitor methyl [(3r,7s)-7-({(2e)-3- [5-chloro-2-(1h-tetrazol-1-yl)phenyl]prop-2-enoyl}amino)-3-ethyl-2- oxo-1,2,3,4,5,6,7,9-octahydro-11,8-(azeno)-1,9- benzodiazacyclotridecin-14-yl]carbamate

Structure deposition date

2017-05-01

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

514

Residue number B

581

Peptide name

Coagulation factor XI

Ligandability

Cysteine 514 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 581 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 291 and 374 (273 and 356 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

crystal structure at 2

Structure deposition date

2005-12-01

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

291

Residue number B

374

Peptide name

Coagulation factor XI

Ligandability

Cysteine 291 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 374 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 317 and 346 (299 and 328 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

human recombinant coagulation fxi in complex with a peptide derived from human high molecular weight kininogen (hkp)

Structure deposition date

2016-02-08

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

317

Residue number B

346

Peptide name

Coagulation factor XI

Ligandability

Cysteine 317 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 346 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 110 and 193 (92 and 175 respectively in this structure).

Details

Redox score ?

PDB code

6i58

Structure name

allosteric activation of human prekallikrein by apple domain disc rotation

Structure deposition date

2018-11-13

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

110

Residue number B

193

Peptide name

Coagulation factor XI

Ligandability

Cysteine 110 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 193 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 50 and 56 (32 and 38 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes

Structure deposition date

2021-12-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

Residue number B

Peptide name

Coagulation factor XI

Ligandability

Cysteine 50 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 56 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 46 and 76 (28 and 58 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

human recombinant coagulation fxi in complex with a peptide derived from human high molecular weight kininogen (hkp)

Structure deposition date

2016-02-08

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

Residue number B

Peptide name

Coagulation factor XI

Ligandability

Cysteine 46 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 76 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 136 and 165 (118 and 147 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes

Structure deposition date

2021-12-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

136

Residue number B

165

Peptide name

Coagulation factor XI

Ligandability

Cysteine 136 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 165 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 140 and 146 (122 and 128 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes

Structure deposition date

2021-12-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

140

Residue number B

146

Peptide name

Coagulation factor XI

Ligandability

Cysteine 140 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 146 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 321 and 327 (303 and 309 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

crystal structure at 2

Structure deposition date

2005-12-01

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

321

Residue number B

327

Peptide name

Coagulation factor XI

Ligandability

Cysteine 321 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 327 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 545 and 560 (168 and 182 respectively in this structure).

Details

Redox score ?

PDB code

5qtx

Structure name

Structure deposition date

2019-11-13

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

545

Residue number B

560

Peptide name

Coagulation factor XI

Ligandability

Cysteine 545 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 560 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 200 and 283 (182 and 265 respectively in this structure).

Details

Redox score ?

PDB code

6i58

Structure name

allosteric activation of human prekallikrein by apple domain disc rotation

Structure deposition date

2018-11-13

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

200

Residue number B

283

Peptide name

Coagulation factor XI

Ligandability

Cysteine 200 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 283 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 226 and 255 (208 and 237 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

crystal structure at 2

Structure deposition date

2005-12-01

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

226

Residue number B

255

Peptide name

Coagulation factor XI

Ligandability

Cysteine 226 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 255 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 230 and 236 (212 and 218 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes

Structure deposition date

2021-12-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

230

Residue number B

236

Peptide name

Coagulation factor XI

Ligandability

Cysteine 230 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 236 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 416 and 432.

Details

Redox score ?

PDB code

7v0z

Structure name

factor xia in complex with compound 2a

Structure deposition date

2022-05-11

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

Peptide accession

Residue number A

416

Residue number B

432

Peptide name

Coagulation factor XI

Ligandability

Cysteine 416 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 432 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 136 and 140 (118 and 122 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes

Structure deposition date

2021-12-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

136

Residue number B

140

Peptide name

Coagulation factor XI

Ligandability

Cysteine 136 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 140 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 226 and 230 (208 and 212 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

human recombinant coagulation fxi in complex with a peptide derived from human high molecular weight kininogen (hkp)

Structure deposition date

2016-02-08

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

226

Residue number B

230

Peptide name

Coagulation factor XI

Ligandability

Cysteine 226 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 230 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 46 and 50 (28 and 32 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes

Structure deposition date

2021-12-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

Residue number B

Peptide name

Coagulation factor XI

Ligandability

Cysteine 46 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 50 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 321 and 346 (303 and 328 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

human recombinant coagulation fxi in complex with a peptide derived from human high molecular weight kininogen (hkp)

Structure deposition date

2016-02-08

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

321

Residue number B

346

Peptide name

Coagulation factor XI

Ligandability

Cysteine 321 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 346 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 140 and 165 (122 and 147 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes

Structure deposition date

2021-12-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

140

Residue number B

165

Peptide name

Coagulation factor XI

Ligandability

Cysteine 140 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 165 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 56 and 76 (38 and 58 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

crystal structure at 2

Structure deposition date

2005-12-01

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

Residue number B

Peptide name

Coagulation factor XI

Ligandability

Cysteine 56 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 76 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 136 and 146 (118 and 128 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes

Structure deposition date

2021-12-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

136

Residue number B

146

Peptide name

Coagulation factor XI

Ligandability

Cysteine 136 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 146 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 236 and 255 (218 and 237 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

6i58

Structure name

allosteric activation of human prekallikrein by apple domain disc rotation

Structure deposition date

2018-11-13

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

236

Residue number B

255

Peptide name

Coagulation factor XI

Ligandability

Cysteine 236 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 255 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 50 and 76 (32 and 58 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes

Structure deposition date

2021-12-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

Residue number B

Peptide name

Coagulation factor XI

Ligandability

Cysteine 50 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 76 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 46 and 56 (28 and 38 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes

Structure deposition date

2021-12-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

Residue number B

Peptide name

Coagulation factor XI

Ligandability

Cysteine 46 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 56 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 317 and 321 (299 and 303 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes

Structure deposition date

2021-12-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

317

Residue number B

321

Peptide name

Coagulation factor XI

Ligandability

Cysteine 317 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 321 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 327 and 346 (309 and 328 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes

Structure deposition date

2021-12-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

327

Residue number B

346

Peptide name

Coagulation factor XI

Ligandability

Cysteine 327 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 346 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 321 and 374 (303 and 356 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

2j8l

Structure name

fxi apple 4 domain loop-out conformation

Structure deposition date

2006-10-25

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

321

Residue number B

374

Peptide name

Coagulation factor XI

Ligandability

Cysteine 321 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 374 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 291 and 327 (273 and 309 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

2j8l

Structure name

fxi apple 4 domain loop-out conformation

Structure deposition date

2006-10-25

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

291

Residue number B

327

Peptide name

Coagulation factor XI

Ligandability

Cysteine 291 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 327 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 230 and 255 (212 and 237 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

factor xi and plasma kallikrein apple domain structures reveals different kininogen bound complexes

Structure deposition date

2021-12-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

230

Residue number B

255

Peptide name

Coagulation factor XI

Ligandability

Cysteine 230 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 255 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 317 and 327 (299 and 309 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5eok

Structure name

human plasma coagulation factor xi in complex with peptide p39

Structure deposition date

2015-11-10

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

317

Residue number B

327

Peptide name

Coagulation factor XI

Ligandability

Cysteine 317 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 327 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 146 and 165 (128 and 147 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5eok

Structure name

human plasma coagulation factor xi in complex with peptide p39

Structure deposition date

2015-11-10

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

146

Residue number B

165

Peptide name

Coagulation factor XI

Ligandability

Cysteine 146 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 165 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Coagulation factor XI between cysteines 226 and 236 (208 and 218 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5eok

Structure name

human plasma coagulation factor xi in complex with peptide p39

Structure deposition date

2015-11-10

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

226

Residue number B

236

Peptide name

Coagulation factor XI

Ligandability

Cysteine 226 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.

Cysteine 236 of Coagulation factor XI

Not ligandable in the dataset of Vinogradova et al.