Fibrinogen gamma-B chain

Peptide B accession

Peptide A residue number

227

Peptide B residue number

165

Ligandability

Cysteine 227 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 165 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Fibrinogen gamma-B chain at cysteines 32 and 33 (8 and 9 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

crystal structure of the central region of bovine fibrinogen (e5 fragment) at 1

Structure deposition date

2001-09-10

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen gamma-B chain

Peptide B name

Fibrinogen gamma-B chain

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

Ligandability

Cysteine 32 of Fibrinogen gamma-B chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 33 of Fibrinogen gamma-B chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 180 of Fibrinogen alpha chain and cysteine 161 of Fibrinogen gamma chain (161 and 135 respectively in this structure).

Details

Redox score ?

PDB code

2hpc

Structure name

crystal structure of fragment d from human fibrinogen complexed with gly-pro-arg-pro-amide

Structure deposition date

2006-07-17

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen alpha chain

Peptide B name

Fibrinogen gamma chain

Peptide A accession

Peptide B accession

Peptide A residue number

180

Peptide B residue number

161

Ligandability

Cysteine 180 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 161 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 223 of Fibrinogen beta chain and cysteine 161 of Fibrinogen gamma chain (193 and 135 respectively in this structure).

Details

Redox score ?

PDB code

2ffd

Structure name

fibrinogen fragment d with "a" knob peptide mimic gprvve

Structure deposition date

2005-12-19

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen beta chain

Peptide B name

Fibrinogen gamma chain

Peptide A accession

Peptide B accession

Peptide A residue number

223

Peptide B residue number

161

Ligandability

Cysteine 223 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 161 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 110 of Fibrinogen beta chain and cysteine 45 of Fibrinogen gamma chain (80 and 19 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

crystal structure of human fibrinogen

Structure deposition date

2009-03-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen beta chain

Peptide B name

Fibrinogen gamma chain

Peptide A accession

Peptide B accession

Peptide A residue number

110

Peptide B residue number

Ligandability

Cysteine 110 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 45 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 64 of Fibrinogen alpha chain and cysteine 49 of Fibrinogen gamma chain (45 and 23 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

crystal structure of human fibrinogen

Structure deposition date

2009-03-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen alpha chain

Peptide B name

Fibrinogen gamma chain

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

Ligandability

Cysteine 64 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 49 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 184 of Fibrinogen alpha chain and cysteine 161 of Fibrinogen gamma chain (165 and 135 respectively in this structure).

Details

Redox score ?

PDB code

1fzc

Structure name

crystal structure of fragment double-d from human fibrin with two different bound ligands

Structure deposition date

1998-05-19

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen alpha chain

Peptide B name

Fibrinogen gamma chain

Peptide A accession

Peptide B accession

Peptide A residue number

184

Peptide B residue number

161

Ligandability

Cysteine 184 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 161 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Fibrinogen gamma-B chain at cysteines 32 and 32 (8 and 8 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

crystal structure of the central region of bovine fibrinogen (e5 fragment) at 1

Structure deposition date

2001-09-10

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen gamma-B chain

Peptide B name

Fibrinogen gamma-B chain

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Fibrinogen gamma chain at cysteines 35 and 35 (9 and 9 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 of human fibrinogen

Structure deposition date

2009-03-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen gamma chain

Peptide B name

Fibrinogen gamma chain

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 110 of Fibrinogen beta chain and cysteine 34 of Fibrinogen gamma chain (80 and 8 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 of the complex between thrombin and the central "e" region of fibrin

Structure deposition date

2005-06-27

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen beta chain

Peptide B name

Fibrinogen gamma chain

Peptide A accession

Peptide B accession

Peptide A residue number

110

Peptide B residue number

Ligandability

Cysteine 110 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 34 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 110 of Fibrinogen beta chain and cysteine 35 of Fibrinogen gamma chain (80 and 9 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 of human fibrinogen

Structure deposition date

2009-03-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen beta chain

Peptide B name

Fibrinogen gamma chain

Peptide A accession

Peptide B accession

Peptide A residue number

110

Peptide B residue number

Ligandability

Cysteine 110 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 35 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Fibrinogen gamma-B chain at cysteines 43 and 32 (19 and 8 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 of the central region of bovine fibrinogen (e5 fragment) at 1

Structure deposition date

2001-09-10

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen gamma-B chain

Peptide B name

Fibrinogen gamma-B chain

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

Ligandability

Cysteine 43 of Fibrinogen gamma-B chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 32 of Fibrinogen gamma-B chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 45 of Fibrinogen gamma chain and cysteine 64 of Fibrinogen alpha chain (19 and 45 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 of the complex between thrombin and the central "e" region of fibrin

Structure deposition date

2005-06-27

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen gamma chain

Peptide B name

Fibrinogen alpha chain

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

Ligandability

Cysteine 45 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 64 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 223 of Fibrinogen beta chain and cysteine 165 of Fibrinogen gamma chain (193 and 139 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

3h32

Structure name

crystal structure of d-dimer from human fibrin complexed with gly-his- arg-pro-tyr-amide

Structure deposition date

2009-04-15

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen beta chain

Peptide B name

Fibrinogen gamma chain

Peptide A accession

Peptide B accession

Peptide A residue number

223

Peptide B residue number

165

Ligandability

Cysteine 223 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 165 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 227 of Fibrinogen beta chain and cysteine 161 of Fibrinogen gamma chain (197 and 135 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

2oyh

Structure name

crystal structure of fragment d of gammad298,301a fibrinogen with the peptide ligand gly-his-arg-pro-amide

Structure deposition date

2007-02-22

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen beta chain

Peptide B name

Fibrinogen gamma chain

Peptide A accession

Peptide B accession

Peptide A residue number

227

Peptide B residue number

161

Ligandability

Cysteine 227 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 161 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 184 of Fibrinogen alpha chain and cysteine 165 of Fibrinogen gamma chain (165 and 139 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

2xnx

Structure name

bc1 fragment of streptococcal m1 protein in complex with human fibrinogen

Structure deposition date

2010-08-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen alpha chain

Peptide B name

Fibrinogen gamma chain

Peptide A accession

Peptide B accession

Peptide A residue number

184

Peptide B residue number

165

Ligandability

Cysteine 184 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 165 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 316 of Fibrinogen beta chain and cysteine 165 of Fibrinogen gamma chain (286 and 139 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

2xny

Structure name

a fragment of streptococcal m1 protein in complex with human fibrinogen

Structure deposition date

2010-08-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen beta chain

Peptide B name

Fibrinogen gamma chain

Peptide A accession

Peptide B accession

Peptide A residue number

316

Peptide B residue number

165

Ligandability

Cysteine 316 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 165 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 231 of Fibrinogen beta chain and cysteine 165 of Fibrinogen gamma chain (201 and 139 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

2oyi

Structure name

crystal structure of fragment d of gammad298,301a fibrinogen with the peptide ligand gly-pro-arg-pro-amide

Structure deposition date

2007-02-22

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen beta chain

Peptide B name

Fibrinogen gamma chain

Peptide A accession

Peptide B accession

Peptide A residue number

231

Peptide B residue number

165

Ligandability

Cysteine 231 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 165 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 55 of Fibrinogen alpha chain and cysteine 49 of Fibrinogen gamma chain (36 and 23 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 of human fibrinogen

Structure deposition date

2009-03-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen alpha chain

Peptide B name

Fibrinogen gamma chain

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

Ligandability

Cysteine 55 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 49 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 180 of Fibrinogen alpha chain and cysteine 165 of Fibrinogen gamma chain (161 and 139 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

2hpc

Structure name

crystal structure of fragment d from human fibrinogen complexed with gly-pro-arg-pro-amide

Structure deposition date

2006-07-17

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen alpha chain

Peptide B name

Fibrinogen gamma chain

Peptide A accession

Peptide B accession

Peptide A residue number

180

Peptide B residue number

165

Ligandability

Cysteine 180 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 165 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Fibrinogen gamma chain at cysteines 49 and 45 (23 and 19 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 of human fibrinogen

Structure deposition date

2009-03-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen gamma chain

Peptide B name

Fibrinogen gamma chain

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

Ligandability

Cysteine 49 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 45 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Fibrinogen gamma chain at cysteines 35 and 45 (9 and 19 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 of human fibrinogen

Structure deposition date

2009-03-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen gamma chain

Peptide B name

Fibrinogen gamma chain

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

Ligandability

Cysteine 35 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 45 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 49 of Fibrinogen gamma chain and cysteine 95 of Fibrinogen beta chain (23 and 65 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 of the complex between thrombin and the central "e" region of fibrin

Structure deposition date

2005-06-27

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen gamma chain

Peptide B name

Fibrinogen beta chain

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

Ligandability

Cysteine 49 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 95 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Fibrinogen gamma-B chain at cysteines 43 and 43 (19 and 19 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 of the central region of bovine fibrinogen (e5 fragment) at 1

Structure deposition date

2001-09-10

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen gamma-B chain

Peptide B name

Fibrinogen gamma-B chain

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Fibrinogen gamma chain between cysteines 179 and 208 (153 and 182 respectively in this structure).

Details

Redox score ?

PDB code

2hlo

Structure name

crystal structure of fragment d-dimer from human fibrin complexed with gly-hydroxypro-arg-pro-amide

Structure deposition date

2006-07-08

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

179

Residue number B

208

Peptide name

Fibrinogen gamma chain

Ligandability

Cysteine 179 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 208 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Fibrinogen gamma chain between cysteines 352 and 365 (326 and 339 respectively in this structure).

Details

Redox score ?

PDB code

2hpc

Structure name

crystal structure of fragment d from human fibrinogen complexed with gly-pro-arg-pro-amide

Structure deposition date

2006-07-17

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

352

Residue number B

365

Peptide name

Fibrinogen gamma chain

Ligandability

Cysteine 352 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 365 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Fibrinogen gamma chain between cysteines 34 and 35 (8 and 9 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

crystal structure of the complex between thrombin and the central "e" region of fibrin

Structure deposition date

2005-06-27

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

Residue number B

Peptide name

Fibrinogen gamma chain

Ligandability

Cysteine 34 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 35 of Fibrinogen gamma chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Fibrinogen gamma-B chain between cysteines 33 and 43 (9 and 19 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

1jy2

Structure name

crystal structure of the central region of bovine fibrinogen (e5 fragment) at 1

Structure deposition date

2001-09-10

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

Residue number B

Peptide name

Fibrinogen gamma-B chain

Ligandability

Cysteine 33 of Fibrinogen gamma-B chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 43 of Fibrinogen gamma-B chain

Not ligandable in the dataset of Vinogradova et al.