ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Intercellular adhesion molecule 5

Intramolecular
Cysteine 59 and cysteine 103
Cysteine 55 and cysteine 99
Cysteine 344 and cysteine 383
Cysteine 142 and cysteine 198
Cysteine 249 and cysteine 302
A redox-regulated disulphide may form within Intercellular adhesion molecule 5 between cysteines 59 and 103 (28 and 72 respectively in this structure).

Details

Redox score ?
89
PDB code
4oia
Structure name
crystal structure of icam-5 d1-d4 ectodomain fragment, space group p4322
Structure deposition date
2014-01-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMF0
Residue number A
59
Residue number B
103
Peptide name
Intercellular adhesion molecule 5

Ligandability

Cysteine 59 of Intercellular adhesion molecule 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 103 of Intercellular adhesion molecule 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Intercellular adhesion molecule 5 between cysteines 55 and 99 (24 and 68 respectively in this structure).

Details

Redox score ?
84
PDB code
4oia
Structure name
crystal structure of icam-5 d1-d4 ectodomain fragment, space group p4322
Structure deposition date
2014-01-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMF0
Residue number A
55
Residue number B
99
Peptide name
Intercellular adhesion molecule 5

Ligandability

Cysteine 55 of Intercellular adhesion molecule 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 99 of Intercellular adhesion molecule 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Intercellular adhesion molecule 5 between cysteines 344 and 383 (313 and 352 respectively in this structure).

Details

Redox score ?
83
PDB code
4oib
Structure name
crystal structure of icam-5 d1-d4 ectodomain fragment, space group r3
Structure deposition date
2014-01-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMF0
Residue number A
344
Residue number B
383
Peptide name
Intercellular adhesion molecule 5

Ligandability

Cysteine 344 of Intercellular adhesion molecule 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 383 of Intercellular adhesion molecule 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Intercellular adhesion molecule 5 between cysteines 142 and 198 (111 and 167 respectively in this structure).

Details

Redox score ?
82
PDB code
4oia
Structure name
crystal structure of icam-5 d1-d4 ectodomain fragment, space group p4322
Structure deposition date
2014-01-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMF0
Residue number A
142
Residue number B
198
Peptide name
Intercellular adhesion molecule 5

Ligandability

Cysteine 142 of Intercellular adhesion molecule 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 198 of Intercellular adhesion molecule 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Intercellular adhesion molecule 5 between cysteines 249 and 302 (218 and 271 respectively in this structure).

Details

Redox score ?
82
PDB code
4oia
Structure name
crystal structure of icam-5 d1-d4 ectodomain fragment, space group p4322
Structure deposition date
2014-01-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UMF0
Residue number A
249
Residue number B
302
Peptide name
Intercellular adhesion molecule 5

Ligandability

Cysteine 249 of Intercellular adhesion molecule 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 302 of Intercellular adhesion molecule 5

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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