Protein disulfide-isomerase
Intermolecular
Cysteine 529 of Prolyl 4-hydroxylase subunit alpha-2 and cysteine 53 L
Cysteine 311 of Prolyl 4-hydroxylase subunit alpha-2 and cysteine 397 L
Cysteine 529 of Prolyl 4-hydroxylase subunit alpha-2 and cysteine 56
Cysteine 311 of Prolyl 4-hydroxylase subunit alpha-2 and cysteine 400 L
Cysteine 397 and cysteine 866 of Microsomal triglyceride transfer protein large subunit L
Cysteine 400 and cysteine 866 of Microsomal triglyceride transfer protein large subunit L
Intramolecular
Cysteine 53 and cysteine 56 L
Cysteine 397 and cysteine 400 L
7zsc B 529 D 53
A redox-regulated disulphide may form between cysteine 529 of Prolyl 4-hydroxylase subunit alpha-2 and cysteine 53 of Protein disulfide-isomerase.
Details
Redox score ?
86
PDB code
7zsc
Structure name
crystal structure of the heterodimeric human c-p4h-ii with truncated alpha subunit (c-p4h-ii delta281)
Structure deposition date
2022-05-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide A name
Prolyl 4-hydroxylase subunit alpha-2
Peptide B name
Protein disulfide-isomerase
Peptide A accession
O15460
Peptide B accession
P07237
Peptide A residue number
529
Peptide B residue number
53
Ligandability
Cysteine 529 of Prolyl 4-hydroxylase subunit alpha-2
Cysteine 53 of Protein disulfide-isomerase
7zsc A 311 C 397
A redox-regulated disulphide may form between cysteine 311 of Prolyl 4-hydroxylase subunit alpha-2 and cysteine 397 of Protein disulfide-isomerase.
Details
Redox score ?
85
PDB code
7zsc
Structure name
crystal structure of the heterodimeric human c-p4h-ii with truncated alpha subunit (c-p4h-ii delta281)
Structure deposition date
2022-05-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide A name
Prolyl 4-hydroxylase subunit alpha-2
Peptide B name
Protein disulfide-isomerase
Peptide A accession
O15460
Peptide B accession
P07237
Peptide A residue number
311
Peptide B residue number
397
Ligandability
Cysteine 311 of Prolyl 4-hydroxylase subunit alpha-2
Cysteine 397 of Protein disulfide-isomerase
7zsc A 529 C 56
A redox-regulated disulphide may form between cysteine 529 of Prolyl 4-hydroxylase subunit alpha-2 and cysteine 56 of Protein disulfide-isomerase. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
7zsc
Structure name
crystal structure of the heterodimeric human c-p4h-ii with truncated alpha subunit (c-p4h-ii delta281)
Structure deposition date
2022-05-06
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
13
% buried
nan
Peptide A name
Prolyl 4-hydroxylase subunit alpha-2
Peptide B name
Protein disulfide-isomerase
Peptide A accession
O15460
Peptide B accession
P07237
Peptide A residue number
529
Peptide B residue number
56
Ligandability
Cysteine 529 of Prolyl 4-hydroxylase subunit alpha-2
Cysteine 56 of Protein disulfide-isomerase
7zsc A 311 C 400
A redox-regulated disulphide may form between cysteine 311 of Prolyl 4-hydroxylase subunit alpha-2 and cysteine 400 of Protein disulfide-isomerase. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
7zsc
Structure name
crystal structure of the heterodimeric human c-p4h-ii with truncated alpha subunit (c-p4h-ii delta281)
Structure deposition date
2022-05-06
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
13
% buried
nan
Peptide A name
Prolyl 4-hydroxylase subunit alpha-2
Peptide B name
Protein disulfide-isomerase
Peptide A accession
O15460
Peptide B accession
P07237
Peptide A residue number
311
Peptide B residue number
400
Ligandability
Cysteine 311 of Prolyl 4-hydroxylase subunit alpha-2
Cysteine 400 of Protein disulfide-isomerase
6i7s B 397 H 866
A redox-regulated disulphide may form between cysteine 397 of Protein disulfide-isomerase and cysteine 866 of Microsomal triglyceride transfer protein large subunit. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
6i7s
Structure name
microsomal triglyceride transfer protein
Structure deposition date
2018-11-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
9
% buried
84
Peptide A name
Protein disulfide-isomerase
Peptide B name
Microsomal triglyceride transfer protein large subunit
Peptide A accession
P07237
Peptide B accession
P55157
Peptide A residue number
397
Peptide B residue number
866
Ligandability
Cysteine 397 of Protein disulfide-isomerase
Cysteine 866 of Microsomal triglyceride transfer protein large subunit
6i7s A 400 G 866
A redox-regulated disulphide may form between cysteine 400 of Protein disulfide-isomerase and cysteine 866 of Microsomal triglyceride transfer protein large subunit. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
6i7s
Structure name
microsomal triglyceride transfer protein
Structure deposition date
2018-11-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
86
Peptide A name
Protein disulfide-isomerase
Peptide B name
Microsomal triglyceride transfer protein large subunit
Peptide A accession
P07237
Peptide B accession
P55157
Peptide A residue number
400
Peptide B residue number
866
Ligandability
Cysteine 400 of Protein disulfide-isomerase
Cysteine 866 of Microsomal triglyceride transfer protein large subunit
6i7s B 53 B 56
A redox-regulated disulphide may form within Protein disulfide-isomerase between cysteines 53 and 56.
Details
Redox score ?
81
PDB code
6i7s
Structure name
microsomal triglyceride transfer protein
Structure deposition date
2018-11-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
82
Peptide accession
P07237
Residue number A
53
Residue number B
56
Peptide name
Protein disulfide-isomerase
Ligandability
Cysteine 53 of Protein disulfide-isomerase
Cysteine 56 of Protein disulfide-isomerase
6i7s B 397 B 400
A redox-regulated disulphide may form within Protein disulfide-isomerase between cysteines 397 and 400.
Details
Redox score ?
78
PDB code
6i7s
Structure name
microsomal triglyceride transfer protein
Structure deposition date
2018-11-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
67
Minimum pKa ?
9
% buried
79
Peptide accession
P07237
Residue number A
397
Residue number B
400
Peptide name
Protein disulfide-isomerase
Ligandability
Cysteine 397 of Protein disulfide-isomerase
Cysteine 400 of Protein disulfide-isomerase
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