Fibrinogen beta chain

Peptide B accession

Peptide A residue number

184

Peptide B residue number

223

Ligandability

Cysteine 184 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 223 of Fibrinogen beta 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 165 of Fibrinogen gamma chain (197 and 139 respectively in this structure).

Details

Redox score ?

PDB code

2z4e

Structure name

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

Structure deposition date

2007-06-16

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

Q53Y18

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 cysteine 55 of Fibrinogen alpha chain and cysteine 95 of Fibrinogen beta chain (36 and 65 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 A name

Fibrinogen alpha chain

Peptide B name

Fibrinogen beta 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 95 of Fibrinogen beta 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 68 of Fibrinogen alpha chain and cysteine 106 of Fibrinogen beta chain (49 and 76 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 beta chain

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

106

Ligandability

Cysteine 68 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 106 of Fibrinogen beta 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 180 of Fibrinogen alpha chain and cysteine 223 of Fibrinogen beta chain (161 and 193 respectively in this structure).

Details

Redox score ?

PDB code

2hod

Structure name

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

Structure deposition date

2006-07-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen alpha chain

Peptide B name

Fibrinogen beta chain

Peptide A accession

Peptide B accession

Peptide A residue number

180

Peptide B residue number

223

Ligandability

Cysteine 180 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 223 of Fibrinogen beta 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 227 of Fibrinogen beta chain (165 and 197 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

2h43

Structure name

crystal structure of human fragment d complexed with ala-his-arg-pro- amide

Structure deposition date

2006-05-23

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen alpha chain

Peptide B name

Fibrinogen beta chain

Peptide A accession

Peptide B accession

Peptide A residue number

184

Peptide B residue number

227

Ligandability

Cysteine 184 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 227 of Fibrinogen beta 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 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 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 47 of Fibrinogen alpha chain and cysteine 106 of Fibrinogen beta chain (28 and 76 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 beta chain

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

106

Ligandability

Cysteine 47 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 106 of Fibrinogen beta 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 180 of Fibrinogen alpha chain and cysteine 227 of Fibrinogen beta chain (161 and 197 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

1fzb

Structure name

crystal structure of crosslinked fragment d

Structure deposition date

1997-08-05

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Fibrinogen alpha chain

Peptide B name

Fibrinogen beta chain

Peptide A accession

Peptide B accession

Peptide A residue number

180

Peptide B residue number

227

Ligandability

Cysteine 180 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 227 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 68 of Fibrinogen alpha chain and cysteine 95 of Fibrinogen beta chain (49 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 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 beta chain

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

Ligandability

Cysteine 68 of Fibrinogen alpha 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 beta chain at cysteines 106 and 106 (76 and 76 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 beta chain

Peptide A accession

Peptide B accession

Peptide A residue number

106

Peptide B residue number

106

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 55 of Fibrinogen alpha chain and cysteine 106 of Fibrinogen beta chain (36 and 76 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 alpha chain

Peptide B name

Fibrinogen beta chain

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

106

Ligandability

Cysteine 55 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 106 of Fibrinogen beta 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 110 of Fibrinogen beta chain (45 and 80 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 beta chain

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

110

Ligandability

Cysteine 64 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 110 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 95 of Fibrinogen beta chain and cysteine 64 of Fibrinogen alpha chain (65 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 beta chain

Peptide B name

Fibrinogen alpha chain

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

Ligandability

Cysteine 95 of Fibrinogen beta 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 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 cysteine 106 of Fibrinogen beta chain and cysteine 64 of Fibrinogen alpha chain (76 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 beta chain

Peptide B name

Fibrinogen alpha chain

Peptide A accession

Peptide B accession

Peptide A residue number

106

Peptide B residue number

Ligandability

Cysteine 106 of Fibrinogen beta 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 within Fibrinogen beta chain between cysteines 231 and 316 (201 and 286 respectively in this structure).

Details

Redox score ?

PDB code

1re4

Structure name

crystal structure of fragment d of bbetad398a fibrinogen

Structure deposition date

2003-11-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

231

Residue number B

316

Peptide name

Fibrinogen beta chain

Ligandability

Cysteine 231 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 316 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Fibrinogen beta chain between cysteines 241 and 270 (211 and 240 respectively in this structure).

Details

Redox score ?

PDB code

1fzf

Structure name

crystal structure of fragment double-d from human fibrin with the peptide ligand gly-his-arg-pro-amide

Structure deposition date

1998-12-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

241

Residue number B

270

Peptide name

Fibrinogen beta chain

Ligandability

Cysteine 241 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 270 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Fibrinogen beta chain between cysteines 424 and 437 (394 and 407 respectively in this structure).

Details

Redox score ?

PDB code

2hod

Structure name

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

Structure deposition date

2006-07-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

424

Residue number B

437

Peptide name

Fibrinogen beta chain

Ligandability

Cysteine 424 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 437 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Fibrinogen beta chain between cysteines 223 and 227 (193 and 197 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

1fzg

Structure name

crystal structure of fragment d from human fibrinogen with the peptide ligand gly-his-arg-pro-amide

Structure deposition date

1999-01-01

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

223

Residue number B

227

Peptide name

Fibrinogen beta chain

Ligandability

Cysteine 223 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 227 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Fibrinogen beta chain between cysteines 227 and 231 (197 and 201 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 accession

Residue number A

227

Residue number B

231

Peptide name

Fibrinogen beta chain

Ligandability

Cysteine 227 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 231 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Fibrinogen beta chain between cysteines 227 and 316 (197 and 286 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 accession

Residue number A

227

Residue number B

316

Peptide name

Fibrinogen beta chain

Ligandability

Cysteine 227 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 316 of Fibrinogen beta chain

Not ligandable in the dataset of Vinogradova et al.