IgG H chain
Intermolecular
Cysteine 239 and cysteine 107 of Immunoglobulin kappa constant
Cysteine 239 of Ig-like domain-containing protein and cysteine 239
Intramolecular
Cysteine 386 and cysteine 115
Cysteine 163 and cysteine 219
Cysteine 41 and cysteine 115
Cysteine 219 and cysteine 52
5veb A 221 B 215
A redox-regulated disulphide may form between cysteine 239 of IgG H chain and cysteine 107 of Immunoglobulin kappa constant (221 and 215 respectively in this structure).
Details
Redox score ?
94
PDB code
5veb
Structure name
crystal structure of a fab binding to extracellular domain 5 of cadherin-6
Structure deposition date
2017-04-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
IgG H chain
Peptide B name
Immunoglobulin kappa constant
Peptide A accession
S6B291
Peptide B accession
P01834
Peptide A residue number
239
Peptide B residue number
107
Ligandability
Cysteine 239 of IgG H chain
Cysteine 107 of Immunoglobulin kappa constant
5vqm L 214 H 222
A redox-regulated disulphide may form between cysteine 239 of Ig-like domain-containing protein and cysteine 239 of IgG H chain (214 and 222 respectively in this structure).
Details
Redox score ?
82
PDB code
5vqm
Structure name
clostridium difficile tcdb-gtd bound to pa41 fab
Structure deposition date
2017-05-09
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
0
Peptide A name
Ig-like domain-containing protein
Peptide B name
IgG H chain
Peptide A accession
Q8TCD0
Peptide B accession
S6B291
Peptide A residue number
239
Peptide B residue number
239
Ligandability
Cysteine 239 of Ig-like domain-containing protein
Cysteine 239 of IgG H chain
5d9q N 22 N 92
A redox-regulated disulphide may form within IgG H chain between cysteines 386 and 115 (22 and 92 respectively in this structure).
Details
Redox score ?
81
PDB code
5d9q
Structure name
crystal structure of the bg505 sosip gp140 hiv-1 env trimer in complex with the broadly neutralizing fab pgt122 and scfv nih45-46
Structure deposition date
2015-08-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
S6B291
Residue number A
386
Residue number B
115
Peptide name
IgG H chain
Ligandability
Cysteine 386 of IgG H chain
Cysteine 115 of IgG H chain
6ute C 140 C 196
A redox-regulated disulphide may form within IgG H chain between cysteines 163 and 219 (140 and 196 respectively in this structure).
Details
Redox score ?
80
PDB code
6ute
Structure name
crystal structure of z032 fab in complex with wnv ediii
Structure deposition date
2019-10-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
S6B291
Residue number A
163
Residue number B
219
Peptide name
IgG H chain
Ligandability
Cysteine 163 of IgG H chain
Cysteine 219 of IgG H chain
5cus K 22 K 96
A redox-regulated disulphide may form within IgG H chain between cysteines 41 and 115 (22 and 96 respectively in this structure).
Details
Redox score ?
79
PDB code
5cus
Structure name
crystal structure of serbb3-fab3379 complex
Structure deposition date
2015-07-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
S6B291
Residue number A
41
Residue number B
115
Peptide name
IgG H chain
Ligandability
Cysteine 41 of IgG H chain
Cysteine 115 of IgG H chain
5c7k A 32 A 52
A redox-regulated disulphide may form within IgG H chain between cysteines 219 and 52 (32 and 52 respectively in this structure).
Details
Redox score ?
nan
PDB code
5c7k
Structure name
crystal structure bg505 sosip gp140 hiv-1 env trimer bound to broadly neutralizing antibodies pgt128 and 8anc195
Structure deposition date
2015-06-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
S6B291
Residue number A
219
Residue number B
52
Peptide name
IgG H chain
Ligandability
Cysteine 219 of IgG H chain
Cysteine 52 of IgG H chain
Uncertain whether structure cysteine 32 has been assigned to correct residue.
Cysteine 52 in protein B could not be asigned to a Uniprot residue.
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