NAD-capped RNA hydrolase NUDT12
Intermolecular
Cysteine 400 and cysteine 117
Cysteine 387 and cysteine 400
Intramolecular
Cysteine 287 and cysteine 302
Cysteine 302 and cysteine 307
Cysteine 117 and cysteine 387
Cysteine 177 and cysteine 247
Cysteine 287 and cysteine 307
Cysteine 284 and cysteine 307
Cysteine 284 and cysteine 287
Cysteine 284 and cysteine 302
More...Cysteine 337 and cysteine 352
Cysteine 387 and cysteine 400
6scx A 400 B 117
A redox-regulated disulphide may form between two units of NAD-capped RNA hydrolase NUDT12 at cysteines 400 and 117. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
6scx
Structure name
crystal structure of the catalytic domain of human nudt12 in complex with 7-methyl-guanosine-5'-triphosphate
Structure deposition date
2019-07-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
13
% buried
nan
Peptide A name
NAD-capped RNA hydrolase NUDT12
Peptide B name
NAD-capped RNA hydrolase NUDT12
Peptide A accession
Q9BQG2
Peptide B accession
Q9BQG2
Peptide A residue number
400
Peptide B residue number
117
Ligandability
Cysteine 400 of NAD-capped RNA hydrolase NUDT12
Cysteine 117 of NAD-capped RNA hydrolase NUDT12
6scx A 387 B 400
A redox-regulated disulphide may form between two units of NAD-capped RNA hydrolase NUDT12 at cysteines 387 and 400. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
6scx
Structure name
crystal structure of the catalytic domain of human nudt12 in complex with 7-methyl-guanosine-5'-triphosphate
Structure deposition date
2019-07-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
nan
Peptide A name
NAD-capped RNA hydrolase NUDT12
Peptide B name
NAD-capped RNA hydrolase NUDT12
Peptide A accession
Q9BQG2
Peptide B accession
Q9BQG2
Peptide A residue number
387
Peptide B residue number
400
Ligandability
Cysteine 387 of NAD-capped RNA hydrolase NUDT12
Cysteine 400 of NAD-capped RNA hydrolase NUDT12
6scx C 287 C 302
A redox-regulated disulphide may form within NAD-capped RNA hydrolase NUDT12 between cysteines 287 and 302.
Details
Redox score ?
86
PDB code
6scx
Structure name
crystal structure of the catalytic domain of human nudt12 in complex with 7-methyl-guanosine-5'-triphosphate
Structure deposition date
2019-07-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
7
% buried
0
Peptide accession
Q9BQG2
Residue number A
287
Residue number B
302
Peptide name
NAD-capped RNA hydrolase NUDT12
Ligandability
Cysteine 287 of NAD-capped RNA hydrolase NUDT12
Cysteine 302 of NAD-capped RNA hydrolase NUDT12
6scx B 302 B 307
A redox-regulated disulphide may form within NAD-capped RNA hydrolase NUDT12 between cysteines 302 and 307.
Details
Redox score ?
85
PDB code
6scx
Structure name
crystal structure of the catalytic domain of human nudt12 in complex with 7-methyl-guanosine-5'-triphosphate
Structure deposition date
2019-07-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
7
% buried
26
Peptide accession
Q9BQG2
Residue number A
302
Residue number B
307
Peptide name
NAD-capped RNA hydrolase NUDT12
Ligandability
Cysteine 302 of NAD-capped RNA hydrolase NUDT12
Cysteine 307 of NAD-capped RNA hydrolase NUDT12
6scx A 117 A 387
A redox-regulated disulphide may form within NAD-capped RNA hydrolase NUDT12 between cysteines 117 and 387.
Details
Redox score ?
84
PDB code
6scx
Structure name
crystal structure of the catalytic domain of human nudt12 in complex with 7-methyl-guanosine-5'-triphosphate
Structure deposition date
2019-07-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BQG2
Residue number A
117
Residue number B
387
Peptide name
NAD-capped RNA hydrolase NUDT12
Ligandability
Cysteine 117 of NAD-capped RNA hydrolase NUDT12
Cysteine 387 of NAD-capped RNA hydrolase NUDT12
6scx A 177 A 247
A redox-regulated disulphide may form within NAD-capped RNA hydrolase NUDT12 between cysteines 177 and 247.
Details
Redox score ?
83
PDB code
6scx
Structure name
crystal structure of the catalytic domain of human nudt12 in complex with 7-methyl-guanosine-5'-triphosphate
Structure deposition date
2019-07-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BQG2
Residue number A
177
Residue number B
247
Peptide name
NAD-capped RNA hydrolase NUDT12
Ligandability
Cysteine 177 of NAD-capped RNA hydrolase NUDT12
Cysteine 247 of NAD-capped RNA hydrolase NUDT12
6scx B 287 B 307
A redox-regulated disulphide may form within NAD-capped RNA hydrolase NUDT12 between cysteines 287 and 307.
Details
Redox score ?
82
PDB code
6scx
Structure name
crystal structure of the catalytic domain of human nudt12 in complex with 7-methyl-guanosine-5'-triphosphate
Structure deposition date
2019-07-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
19
Peptide accession
Q9BQG2
Residue number A
287
Residue number B
307
Peptide name
NAD-capped RNA hydrolase NUDT12
Ligandability
Cysteine 287 of NAD-capped RNA hydrolase NUDT12
Cysteine 307 of NAD-capped RNA hydrolase NUDT12
6scx B 284 B 307
A redox-regulated disulphide may form within NAD-capped RNA hydrolase NUDT12 between cysteines 284 and 307.
Details
Redox score ?
80
PDB code
6scx
Structure name
crystal structure of the catalytic domain of human nudt12 in complex with 7-methyl-guanosine-5'-triphosphate
Structure deposition date
2019-07-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
42
Peptide accession
Q9BQG2
Residue number A
284
Residue number B
307
Peptide name
NAD-capped RNA hydrolase NUDT12
Ligandability
Cysteine 284 of NAD-capped RNA hydrolase NUDT12
Cysteine 307 of NAD-capped RNA hydrolase NUDT12
6scx A 284 A 287
A redox-regulated disulphide may form within NAD-capped RNA hydrolase NUDT12 between cysteines 284 and 287.
Details
Redox score ?
77
PDB code
6scx
Structure name
crystal structure of the catalytic domain of human nudt12 in complex with 7-methyl-guanosine-5'-triphosphate
Structure deposition date
2019-07-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
6
% buried
38
Peptide accession
Q9BQG2
Residue number A
284
Residue number B
287
Peptide name
NAD-capped RNA hydrolase NUDT12
Ligandability
Cysteine 284 of NAD-capped RNA hydrolase NUDT12
Cysteine 287 of NAD-capped RNA hydrolase NUDT12
6scx B 284 B 302
A redox-regulated disulphide may form within NAD-capped RNA hydrolase NUDT12 between cysteines 284 and 302.
Details
Redox score ?
74
PDB code
6scx
Structure name
crystal structure of the catalytic domain of human nudt12 in complex with 7-methyl-guanosine-5'-triphosphate
Structure deposition date
2019-07-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
45
Peptide accession
Q9BQG2
Residue number A
284
Residue number B
302
Peptide name
NAD-capped RNA hydrolase NUDT12
Ligandability
Cysteine 284 of NAD-capped RNA hydrolase NUDT12
Cysteine 302 of NAD-capped RNA hydrolase NUDT12
6scx B 337 B 352
A redox-regulated disulphide may form within NAD-capped RNA hydrolase NUDT12 between cysteines 337 and 352. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
6scx
Structure name
crystal structure of the catalytic domain of human nudt12 in complex with 7-methyl-guanosine-5'-triphosphate
Structure deposition date
2019-07-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
96
Peptide accession
Q9BQG2
Residue number A
337
Residue number B
352
Peptide name
NAD-capped RNA hydrolase NUDT12
Ligandability
Cysteine 337 of NAD-capped RNA hydrolase NUDT12
Cysteine 352 of NAD-capped RNA hydrolase NUDT12
6o3p A 387 A 400
A redox-regulated disulphide may form within NAD-capped RNA hydrolase NUDT12 between cysteines 387 and 400. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
6o3p
Structure name
crystal structure of the catalytic domain of mouse nudt12 in complex with amp and 3 mg2+ ions
Structure deposition date
2019-02-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
13
% buried
98
Peptide accession
Q9DCN1
Residue number A
387
Residue number B
400
Peptide name
NAD-capped RNA hydrolase NUDT12
Ligandability
Cysteine 387 of NAD-capped RNA hydrolase NUDT12
Cysteine 400 of NAD-capped RNA hydrolase NUDT12
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