ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cobalamin binding intrinsic factor

Intermolecular
Cysteine 103 and cysteine 143
Cysteine 103 and cysteine 182
Intramolecular
Cysteine 26 and cysteine 246
Cysteine 103 and cysteine 288
Cysteine 143 and cysteine 182
A redox-regulated disulphide may form between two units of Cobalamin binding intrinsic factor at cysteines 103 and 143 (85 and 125 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
2pmv
Structure name
crystal structure of human intrinsic factor- cobalamin complex at 2
Structure deposition date
2007-04-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide A name
Cobalamin binding intrinsic factor
Peptide B name
Cobalamin binding intrinsic factor
Peptide A accession
P27352
Peptide B accession
P27352
Peptide A residue number
103
Peptide B residue number
143

Ligandability

Cysteine 103 of Cobalamin binding intrinsic factor

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 143 of Cobalamin binding intrinsic factor

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 between two units of Cobalamin binding intrinsic factor at cysteines 103 and 182 (85 and 164 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
2pmv
Structure name
crystal structure of human intrinsic factor- cobalamin complex at 2
Structure deposition date
2007-04-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide A name
Cobalamin binding intrinsic factor
Peptide B name
Cobalamin binding intrinsic factor
Peptide A accession
P27352
Peptide B accession
P27352
Peptide A residue number
103
Peptide B residue number
182

Ligandability

Cysteine 103 of Cobalamin binding intrinsic factor

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 182 of Cobalamin binding intrinsic factor

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 Cobalamin binding intrinsic factor between cysteines 26 and 246.

Details

Redox score ?
87
PDB code
3kq4
Structure name
structure of intrinsic factor-cobalamin bound to its receptor cubilin
Structure deposition date
2009-11-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27352
Residue number A
26
Residue number B
246
Peptide name
Cobalamin binding intrinsic factor

Ligandability

Cysteine 26 of Cobalamin binding intrinsic factor

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 246 of Cobalamin binding intrinsic factor

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 Cobalamin binding intrinsic factor between cysteines 103 and 288 (85 and 270 respectively in this structure).

Details

Redox score ?
81
PDB code
2pmv
Structure name
crystal structure of human intrinsic factor- cobalamin complex at 2
Structure deposition date
2007-04-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27352
Residue number A
103
Residue number B
288
Peptide name
Cobalamin binding intrinsic factor

Ligandability

Cysteine 103 of Cobalamin binding intrinsic factor

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 288 of Cobalamin binding intrinsic factor

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 Cobalamin binding intrinsic factor between cysteines 143 and 182 (125 and 164 respectively in this structure).

Details

Redox score ?
78
PDB code
2pmv
Structure name
crystal structure of human intrinsic factor- cobalamin complex at 2
Structure deposition date
2007-04-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide accession
P27352
Residue number A
143
Residue number B
182
Peptide name
Cobalamin binding intrinsic factor

Ligandability

Cysteine 143 of Cobalamin binding intrinsic factor

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 182 of Cobalamin binding intrinsic factor

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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