HLA class II histocompatibility antigen gamma chain
Intramolecular
Cysteine 213 and cysteine 232
Cysteine 252 and cysteine 271
Cysteine 243 and cysteine 250
Cysteine 250 and cysteine 271
Cysteine 243 and cysteine 271
Cysteine 250 and cysteine 252
Cysteine 243 and cysteine 252
1icf J 197 J 216
A redox-regulated disulphide may form within HLA class II histocompatibility antigen gamma chain between cysteines 213 and 232 (197 and 216 respectively in this structure).
Details
Redox score ?
87
PDB code
1icf
Structure name
crystal structure of mhc class ii associated p41 ii fragment in complex with cathepsin l
Structure deposition date
1999-01-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04233
Residue number A
213
Residue number B
232
Peptide name
HLA class II histocompatibility antigen gamma chain
Ligandability
Cysteine 213 of HLA class II histocompatibility antigen gamma chain
Cysteine 232 of HLA class II histocompatibility antigen gamma chain
1icf I 236 I 255
A redox-regulated disulphide may form within HLA class II histocompatibility antigen gamma chain between cysteines 252 and 271 (236 and 255 respectively in this structure).
Details
Redox score ?
85
PDB code
1icf
Structure name
crystal structure of mhc class ii associated p41 ii fragment in complex with cathepsin l
Structure deposition date
1999-01-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04233
Residue number A
252
Residue number B
271
Peptide name
HLA class II histocompatibility antigen gamma chain
Ligandability
Cysteine 252 of HLA class II histocompatibility antigen gamma chain
Cysteine 271 of HLA class II histocompatibility antigen gamma chain
1icf J 227 J 234
A redox-regulated disulphide may form within HLA class II histocompatibility antigen gamma chain between cysteines 243 and 250 (227 and 234 respectively in this structure).
Details
Redox score ?
81
PDB code
1icf
Structure name
crystal structure of mhc class ii associated p41 ii fragment in complex with cathepsin l
Structure deposition date
1999-01-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04233
Residue number A
243
Residue number B
250
Peptide name
HLA class II histocompatibility antigen gamma chain
Ligandability
Cysteine 243 of HLA class II histocompatibility antigen gamma chain
Cysteine 250 of HLA class II histocompatibility antigen gamma chain
1icf I 234 I 255
A redox-regulated disulphide may form within HLA class II histocompatibility antigen gamma chain between cysteines 250 and 271 (234 and 255 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
1icf
Structure name
crystal structure of mhc class ii associated p41 ii fragment in complex with cathepsin l
Structure deposition date
1999-01-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04233
Residue number A
250
Residue number B
271
Peptide name
HLA class II histocompatibility antigen gamma chain
Ligandability
Cysteine 250 of HLA class II histocompatibility antigen gamma chain
Cysteine 271 of HLA class II histocompatibility antigen gamma chain
1icf J 227 J 255
A redox-regulated disulphide may form within HLA class II histocompatibility antigen gamma chain between cysteines 243 and 271 (227 and 255 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
1icf
Structure name
crystal structure of mhc class ii associated p41 ii fragment in complex with cathepsin l
Structure deposition date
1999-01-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04233
Residue number A
243
Residue number B
271
Peptide name
HLA class II histocompatibility antigen gamma chain
Ligandability
Cysteine 243 of HLA class II histocompatibility antigen gamma chain
Cysteine 271 of HLA class II histocompatibility antigen gamma chain
1icf J 234 J 236
A redox-regulated disulphide may form within HLA class II histocompatibility antigen gamma chain between cysteines 250 and 252 (234 and 236 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
1icf
Structure name
crystal structure of mhc class ii associated p41 ii fragment in complex with cathepsin l
Structure deposition date
1999-01-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04233
Residue number A
250
Residue number B
252
Peptide name
HLA class II histocompatibility antigen gamma chain
Ligandability
Cysteine 250 of HLA class II histocompatibility antigen gamma chain
Cysteine 252 of HLA class II histocompatibility antigen gamma chain
1icf I 227 I 236
A redox-regulated disulphide may form within HLA class II histocompatibility antigen gamma chain between cysteines 243 and 252 (227 and 236 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
1icf
Structure name
crystal structure of mhc class ii associated p41 ii fragment in complex with cathepsin l
Structure deposition date
1999-01-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04233
Residue number A
243
Residue number B
252
Peptide name
HLA class II histocompatibility antigen gamma chain
Ligandability
Cysteine 243 of HLA class II histocompatibility antigen gamma chain
Cysteine 252 of HLA class II histocompatibility antigen gamma chain
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