Protein disulfide-isomerase A3
Intermolecular
Cysteine 115 of Tapasin and cysteine 57 L
Cysteine 115 of Tapasin and cysteine 60 L
Intramolecular
Cysteine 406 and cysteine 409 L
Cysteine 85 and cysteine 92 L
Cysteine 57 and cysteine 60 L
Cysteine 60 and cysteine 85 L
Cysteine 57 and cysteine 85 L
7qng A 95 B 33
A redox-regulated disulphide may form between cysteine 115 of Tapasin and cysteine 57 of Protein disulfide-isomerase A3 (95 and 33 respectively in this structure).
Details
Redox score ?
83
PDB code
7qng
Structure name
structure of a mhc i-tapasin-erp57 complex
Structure deposition date
2021-12-20
Thiol separation (Å)
3
Half-sphere exposure sum ?
67
Minimum pKa ?
7
% buried
62
Peptide A name
Tapasin
Peptide B name
Protein disulfide-isomerase A3
Peptide A accession
O15533
Peptide B accession
P30101
Peptide A residue number
115
Peptide B residue number
57
Ligandability
Cysteine 115 of Tapasin
Cysteine 57 of Protein disulfide-isomerase A3
7qpd T 95 E 36
A redox-regulated disulphide may form between cysteine 115 of Tapasin and cysteine 60 of Protein disulfide-isomerase A3 (95 and 36 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
7qpd
Structure name
structure of the human mhc i peptide-loading complex editing module
Structure deposition date
2022-01-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
nan
Peptide A name
Tapasin
Peptide B name
Protein disulfide-isomerase A3
Peptide A accession
O15533
Peptide B accession
P30101
Peptide A residue number
115
Peptide B residue number
60
Ligandability
Cysteine 115 of Tapasin
Cysteine 60 of Protein disulfide-isomerase A3
2dmm A 57 A 60
A redox-regulated disulphide may form within Protein disulfide-isomerase A3 between cysteines 406 and 409 (57 and 60 respectively in this structure).
Details
Redox score ?
85
PDB code
2dmm
Structure name
the solution structure of the second thioredoxin domain of human protein disulfide-isomerase a3
Structure deposition date
2006-04-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
43
Minimum pKa ?
9
% buried
11
Peptide accession
P30101
Residue number A
406
Residue number B
409
Peptide name
Protein disulfide-isomerase A3
Ligandability
Cysteine 406 of Protein disulfide-isomerase A3
Cysteine 409 of Protein disulfide-isomerase A3
2alb A 61 A 68
A redox-regulated disulphide may form within Protein disulfide-isomerase A3 between cysteines 85 and 92 (61 and 68 respectively in this structure).
Details
Redox score ?
79
PDB code
2alb
Structure name
nmr structure of the n-terminal domain a of the glycoprotein chaperone erp57
Structure deposition date
2005-08-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
0
Peptide accession
P30101
Residue number A
85
Residue number B
92
Peptide name
Protein disulfide-isomerase A3
Ligandability
Cysteine 85 of Protein disulfide-isomerase A3
Cysteine 92 of Protein disulfide-isomerase A3
2alb A 33 A 36
A redox-regulated disulphide may form within Protein disulfide-isomerase A3 between cysteines 57 and 60 (33 and 36 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
2alb
Structure name
nmr structure of the n-terminal domain a of the glycoprotein chaperone erp57
Structure deposition date
2005-08-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
41
Minimum pKa ?
9
% buried
4
Peptide accession
P30101
Residue number A
57
Residue number B
60
Peptide name
Protein disulfide-isomerase A3
Ligandability
Cysteine 57 of Protein disulfide-isomerase A3
Cysteine 60 of Protein disulfide-isomerase A3
2alb A 36 A 61
A redox-regulated disulphide may form within Protein disulfide-isomerase A3 between cysteines 60 and 85 (36 and 61 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
2alb
Structure name
nmr structure of the n-terminal domain a of the glycoprotein chaperone erp57
Structure deposition date
2005-08-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
4
Peptide accession
P30101
Residue number A
60
Residue number B
85
Peptide name
Protein disulfide-isomerase A3
Ligandability
Cysteine 60 of Protein disulfide-isomerase A3
Cysteine 85 of Protein disulfide-isomerase A3
2alb A 33 A 61
A redox-regulated disulphide may form within Protein disulfide-isomerase A3 between cysteines 57 and 85 (33 and 61 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
2alb
Structure name
nmr structure of the n-terminal domain a of the glycoprotein chaperone erp57
Structure deposition date
2005-08-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
0
Peptide accession
P30101
Residue number A
57
Residue number B
85
Peptide name
Protein disulfide-isomerase A3
Ligandability
Cysteine 57 of Protein disulfide-isomerase A3
Cysteine 85 of Protein disulfide-isomerase A3
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