Carboxypeptidase O
Intermolecular
Cysteine 177 and cysteine 38 of Metallocarboxypeptidase inhibitor
Cysteine 199 and cysteine 38 of Metallocarboxypeptidase inhibitor
Cysteine 177 and cysteine 27 of Metallocarboxypeptidase inhibitor
Intramolecular
Cysteine 177 and cysteine 199
Cysteine 191 and cysteine 205
Cysteine 105 and cysteine 118
Cysteine 105 and cysteine 330
Cysteine 118 and cysteine 330
5mrv A 157 C 38
A redox-regulated disulphide may form between cysteine 177 of Carboxypeptidase O and cysteine 38 of Metallocarboxypeptidase inhibitor (157 and 38 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
5mrv
Structure name
crystal structure of human carboxypeptidase o in complex with nvci
Structure deposition date
2016-12-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide A name
Carboxypeptidase O
Peptide B name
Metallocarboxypeptidase inhibitor
Peptide A accession
Q8IVL8
Peptide B accession
P86912
Peptide A residue number
177
Peptide B residue number
38
Ligandability
Cysteine 177 of Carboxypeptidase O
Cysteine 38 of Metallocarboxypeptidase inhibitor
5mrv A 179 C 38
A redox-regulated disulphide may form between cysteine 199 of Carboxypeptidase O and cysteine 38 of Metallocarboxypeptidase inhibitor (179 and 38 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
5mrv
Structure name
crystal structure of human carboxypeptidase o in complex with nvci
Structure deposition date
2016-12-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide A name
Carboxypeptidase O
Peptide B name
Metallocarboxypeptidase inhibitor
Peptide A accession
Q8IVL8
Peptide B accession
P86912
Peptide A residue number
199
Peptide B residue number
38
Ligandability
Cysteine 199 of Carboxypeptidase O
Cysteine 38 of Metallocarboxypeptidase inhibitor
5mrv A 157 C 27
A redox-regulated disulphide may form between cysteine 177 of Carboxypeptidase O and cysteine 27 of Metallocarboxypeptidase inhibitor (157 and 27 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
5mrv
Structure name
crystal structure of human carboxypeptidase o in complex with nvci
Structure deposition date
2016-12-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide A name
Carboxypeptidase O
Peptide B name
Metallocarboxypeptidase inhibitor
Peptide A accession
Q8IVL8
Peptide B accession
P86912
Peptide A residue number
177
Peptide B residue number
27
Ligandability
Cysteine 177 of Carboxypeptidase O
Cysteine 27 of Metallocarboxypeptidase inhibitor
5mrv B 157 B 179
A redox-regulated disulphide may form within Carboxypeptidase O between cysteines 177 and 199 (157 and 179 respectively in this structure).
Details
Redox score ?
88
PDB code
5mrv
Structure name
crystal structure of human carboxypeptidase o in complex with nvci
Structure deposition date
2016-12-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
0
Peptide accession
Q8IVL8
Residue number A
177
Residue number B
199
Peptide name
Carboxypeptidase O
Ligandability
Cysteine 177 of Carboxypeptidase O
Cysteine 199 of Carboxypeptidase O
5mrv A 171 A 185
A redox-regulated disulphide may form within Carboxypeptidase O between cysteines 191 and 205 (171 and 185 respectively in this structure).
Details
Redox score ?
80
PDB code
5mrv
Structure name
crystal structure of human carboxypeptidase o in complex with nvci
Structure deposition date
2016-12-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
72
Minimum pKa ?
9
% buried
39
Peptide accession
Q8IVL8
Residue number A
191
Residue number B
205
Peptide name
Carboxypeptidase O
Ligandability
Cysteine 191 of Carboxypeptidase O
Cysteine 205 of Carboxypeptidase O
5mrv A 85 A 98
A redox-regulated disulphide may form within Carboxypeptidase O between cysteines 105 and 118 (85 and 98 respectively in this structure).
Details
Redox score ?
77
PDB code
5mrv
Structure name
crystal structure of human carboxypeptidase o in complex with nvci
Structure deposition date
2016-12-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8IVL8
Residue number A
105
Residue number B
118
Peptide name
Carboxypeptidase O
Ligandability
Cysteine 105 of Carboxypeptidase O
Cysteine 118 of Carboxypeptidase O
5mrv A 85 A 310
A redox-regulated disulphide may form within Carboxypeptidase O between cysteines 105 and 330 (85 and 310 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
5mrv
Structure name
crystal structure of human carboxypeptidase o in complex with nvci
Structure deposition date
2016-12-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
13
% buried
nan
Peptide accession
Q8IVL8
Residue number A
105
Residue number B
330
Peptide name
Carboxypeptidase O
Ligandability
Cysteine 105 of Carboxypeptidase O
Cysteine 330 of Carboxypeptidase O
5mrv B 98 B 310
A redox-regulated disulphide may form within Carboxypeptidase O between cysteines 118 and 330 (98 and 310 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
28
PDB code
5mrv
Structure name
crystal structure of human carboxypeptidase o in complex with nvci
Structure deposition date
2016-12-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
13
% buried
nan
Peptide accession
Q8IVL8
Residue number A
118
Residue number B
330
Peptide name
Carboxypeptidase O
Ligandability
Cysteine 118 of Carboxypeptidase O
Cysteine 330 of Carboxypeptidase O
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