C->U-editing enzyme APOBEC-1
Intramolecular
Cysteine 93 and cysteine 96
Cysteine 184 and cysteine 192
Cysteine 184 and cysteine 213
Cysteine 192 and cysteine 213
Cysteine 37 and cysteine 152
6x91 A 1093 A 1096
A redox-regulated disulphide may form within C->U-editing enzyme APOBEC-1 between cysteines 93 and 96 (1093 and 1096 respectively in this structure).
Details
Redox score ?
85
PDB code
6x91
Structure name
crystal structure of mbp-fused human apobec1
Structure deposition date
2020-06-02
Thiol separation (Å)
3
Half-sphere exposure sum ?
62
Minimum pKa ?
4
% buried
61
Peptide accession
P41238
Residue number A
93
Residue number B
96
Peptide name
C->U-editing enzyme APOBEC-1
Ligandability
Cysteine 93 of C->U-editing enzyme APOBEC-1
Cysteine 96 of C->U-editing enzyme APOBEC-1
6x91 G 1184 G 1192
A redox-regulated disulphide may form within C->U-editing enzyme APOBEC-1 between cysteines 184 and 192 (1184 and 1192 respectively in this structure).
Details
Redox score ?
79
PDB code
6x91
Structure name
crystal structure of mbp-fused human apobec1
Structure deposition date
2020-06-02
Thiol separation (Å)
3
Half-sphere exposure sum ?
71
Minimum pKa ?
6
% buried
90
Peptide accession
P41238
Residue number A
184
Residue number B
192
Peptide name
C->U-editing enzyme APOBEC-1
Ligandability
Cysteine 184 of C->U-editing enzyme APOBEC-1
Cysteine 192 of C->U-editing enzyme APOBEC-1
6x91 H 1184 H 1213
A redox-regulated disulphide may form within C->U-editing enzyme APOBEC-1 between cysteines 184 and 213 (1184 and 1213 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
6x91
Structure name
crystal structure of mbp-fused human apobec1
Structure deposition date
2020-06-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
6
% buried
41
Peptide accession
P41238
Residue number A
184
Residue number B
213
Peptide name
C->U-editing enzyme APOBEC-1
Ligandability
Cysteine 184 of C->U-editing enzyme APOBEC-1
Cysteine 213 of C->U-editing enzyme APOBEC-1
6x91 G 1192 G 1213
A redox-regulated disulphide may form within C->U-editing enzyme APOBEC-1 between cysteines 192 and 213 (1192 and 1213 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
6x91
Structure name
crystal structure of mbp-fused human apobec1
Structure deposition date
2020-06-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
6
% buried
64
Peptide accession
P41238
Residue number A
192
Residue number B
213
Peptide name
C->U-editing enzyme APOBEC-1
Ligandability
Cysteine 192 of C->U-editing enzyme APOBEC-1
Cysteine 213 of C->U-editing enzyme APOBEC-1
6x91 C 1037 C 1152
A redox-regulated disulphide may form within C->U-editing enzyme APOBEC-1 between cysteines 37 and 152 (1037 and 1152 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
6x91
Structure name
crystal structure of mbp-fused human apobec1
Structure deposition date
2020-06-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
11
% buried
100
Peptide accession
P41238
Residue number A
37
Residue number B
152
Peptide name
C->U-editing enzyme APOBEC-1
Ligandability
Cysteine 37 of C->U-editing enzyme APOBEC-1
Cysteine 152 of C->U-editing enzyme APOBEC-1
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