ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

IgG receptor FcRn large subunit p51

Intramolecular
Cysteine 221 and cysteine 275
Cysteine 119 and cysteine 182
Cysteine 221 and cysteine 274
Cysteine 274 and cysteine 275
Cysteine 71 and cysteine 301
Cysteine 70 and cysteine 901
Cysteine 248 and cysteine 951
A redox-regulated disulphide may form within IgG receptor FcRn large subunit p51 between cysteines 221 and 275 (198 and 252 respectively in this structure).

Details

Redox score ?
73
PDB code
6la7
Structure name
cryo-em structure of echovirus 11 complexed with its uncoating receptor fcrn at ph 5
Structure deposition date
2019-11-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
84
Minimum pKa ?
8
% buried
81
Peptide accession
P55899
Residue number A
221
Residue number B
275
Peptide name
IgG receptor FcRn large subunit p51

Ligandability

Cysteine 221 of IgG receptor FcRn large subunit p51

Cysteine 275 of IgG receptor FcRn large subunit p51

A redox-regulated disulphide may form within IgG receptor FcRn large subunit p51 between cysteines 119 and 182 (96 and 159 respectively in this structure).

Details

Redox score ?
69
PDB code
6c97
Structure name
crystal structure of fcrn at ph3
Structure deposition date
2018-01-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
41
Peptide accession
P55899
Residue number A
119
Residue number B
182
Peptide name
IgG receptor FcRn large subunit p51

Ligandability

Cysteine 119 of IgG receptor FcRn large subunit p51

Cysteine 182 of IgG receptor FcRn large subunit p51

A redox-regulated disulphide may form within IgG receptor FcRn large subunit p51 between cysteines 221 and 274 (198 and 251 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6wna
Structure name
next generation monomeric igg4 fc
Structure deposition date
2020-04-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
nan
Peptide accession
P55899
Residue number A
221
Residue number B
274
Peptide name
IgG receptor FcRn large subunit p51

Ligandability

Cysteine 221 of IgG receptor FcRn large subunit p51

Cysteine 274 of IgG receptor FcRn large subunit p51

A redox-regulated disulphide may form within IgG receptor FcRn large subunit p51 between cysteines 274 and 275 (251 and 252 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
5bxf
Structure name
apo fcrn structure at ph 4
Structure deposition date
2015-06-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
nan
Peptide accession
P55899
Residue number A
274
Residue number B
275
Peptide name
IgG receptor FcRn large subunit p51

Ligandability

Cysteine 274 of IgG receptor FcRn large subunit p51

Cysteine 275 of IgG receptor FcRn large subunit p51

A redox-regulated disulphide may form within IgG receptor FcRn large subunit p51 between cysteines 71 and 301 (48 and 301 respectively in this structure).

Details

Redox score ?
nan
PDB code
6qip
Structure name
ternary complex of fcrn ectodomain, fcrn binding optimised human serum albumin and the albumin-biniding side chain of the human growth hormone derivative somapacitan
Structure deposition date
2019-01-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P55899
Residue number A
71
Residue number B
301
Peptide name
IgG receptor FcRn large subunit p51

Ligandability

Cysteine 71 of IgG receptor FcRn large subunit p51

Cysteine 301 of IgG receptor FcRn large subunit p51

Cysteine 301 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within IgG receptor FcRn large subunit p51 between cysteines 70 and 901 (48 and 901 respectively in this structure).

Details

Redox score ?
nan
PDB code
1i1a
Structure name
crystal structure of the neonatal fc receptor complexed with a heterodimeric fc
Structure deposition date
2001-01-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13599
Residue number A
70
Residue number B
901
Peptide name
IgG receptor FcRn large subunit p51

Ligandability

Cysteine 70 of IgG receptor FcRn large subunit p51

Cysteine 901 of IgG receptor FcRn large subunit p51

Cysteine 901 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within IgG receptor FcRn large subunit p51 between cysteines 248 and 951 (226 and 951 respectively in this structure).

Details

Redox score ?
nan
PDB code
1i1a
Structure name
crystal structure of the neonatal fc receptor complexed with a heterodimeric fc
Structure deposition date
2001-01-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P13599
Residue number A
248
Residue number B
951
Peptide name
IgG receptor FcRn large subunit p51

Ligandability

Cysteine 248 of IgG receptor FcRn large subunit p51

Cysteine 951 of IgG receptor FcRn large subunit p51

Cysteine 951 in protein B could not be asigned to a Uniprot residue.
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