ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

High affinity immunoglobulin gamma Fc receptor I

Intramolecular
Cysteine 212 and cysteine 260
Cysteine 43 and cysteine 85
Cysteine 124 and cysteine 168
A redox-regulated disulphide may form within High affinity immunoglobulin gamma Fc receptor I between cysteines 212 and 260.

Details

Redox score ?
84
PDB code
4x4m
Structure name
structure of fcgammari in complex with fc reveals the importance of glycan recognition for high affinity igg binding
Structure deposition date
2014-12-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P12314
Residue number A
212
Residue number B
260
Peptide name
High affinity immunoglobulin gamma Fc receptor I

Ligandability

Cysteine 212 of High affinity immunoglobulin gamma Fc receptor I

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 260 of High affinity immunoglobulin gamma Fc receptor I

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 High affinity immunoglobulin gamma Fc receptor I between cysteines 43 and 85.

Details

Redox score ?
82
PDB code
3rjd
Structure name
crystal structure of fc ri and its implication to high affinity immunoglobulin g binding
Structure deposition date
2011-04-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P12314
Residue number A
43
Residue number B
85
Peptide name
High affinity immunoglobulin gamma Fc receptor I

Ligandability

Cysteine 43 of High affinity immunoglobulin gamma Fc receptor I

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 85 of High affinity immunoglobulin gamma Fc receptor I

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 High affinity immunoglobulin gamma Fc receptor I between cysteines 124 and 168.

Details

Redox score ?
79
PDB code
4w4o
Structure name
high-resolution crystal structure of fc bound to its human receptor fc-gamma-ri
Structure deposition date
2014-08-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
92
Minimum pKa ?
nan
% buried
nan
Peptide accession
P12314
Residue number A
124
Residue number B
168
Peptide name
High affinity immunoglobulin gamma Fc receptor I

Ligandability

Cysteine 124 of High affinity immunoglobulin gamma Fc receptor I

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 168 of High affinity immunoglobulin gamma Fc receptor I

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.

If this tool was useful for finding a disulphide, please cite: