Fibrinogen alpha chain

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 alpha 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 184 of Fibrinogen alpha chain and cysteine 223 of Fibrinogen beta chain (165 and 193 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 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

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 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

Q53Y18

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 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 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 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 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 two units of Fibrinogen alpha chain at cysteines 68 and 47 (49 and 28 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 alpha 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 47 of Fibrinogen alpha 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 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 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 two units of Fibrinogen alpha chain at cysteines 68 and 55 (49 and 36 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 alpha 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 55 of Fibrinogen alpha 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 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 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

Q53Y18

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 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 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 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 alpha chain between cysteines 455 and 485 (19 and 49 respectively in this structure).

Details

Redox score ?

PDB code

2jor

Structure name

nmr solution structure, stability, and interaction of the recombinant bovine fibrinogen alphac-domain fragment

Structure deposition date

2007-03-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

P02672

Residue number A

455

Residue number B

485

Peptide name

Fibrinogen alpha chain

Ligandability

Cysteine 455 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 485 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Fibrinogen alpha chain between cysteines 799 and 812 (780 and 793 respectively in this structure).

Details

Redox score ?

PDB code

1fzd

Structure name

structure of recombinant alphaec domain from human fibrinogen-420

Structure deposition date

1998-06-22

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

799

Residue number B

812

Peptide name

Fibrinogen alpha chain

Ligandability

Cysteine 799 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 812 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Fibrinogen alpha chain between cysteines 180 and 184 (161 and 165 respectively in this structure).

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 accession

Residue number A

180

Residue number B

184

Peptide name

Fibrinogen alpha chain

Ligandability

Cysteine 180 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.

Cysteine 184 of Fibrinogen alpha chain

Not ligandable in the dataset of Vinogradova et al.