S-adenosylhomocysteine hydrolase-like protein 1
Intramolecular
Cysteine 292 and cysteine 293
Cysteine 106 and cysteine 211
Cysteine 326 and cysteine 327
Cysteine 326 and cysteine 373
Cysteine 151 and cysteine 177
Cysteine 151 and cysteine 215
Cysteine 327 and cysteine 373
Cysteine 317 and cysteine 373
Cysteine 326 and cysteine 395
Cysteine 211 and cysteine 215
More...Cysteine 293 and cysteine 326
Cysteine 172 and cysteine 215
Cysteine 373 and cysteine 395
Cysteine 293 and cysteine 373
Cysteine 317 and cysteine 327
Cysteine 151 and cysteine 211
3mtg A 292 A 293
A redox-regulated disulphide may form within S-adenosylhomocysteine hydrolase-like protein 1 between cysteines 292 and 293. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
3mtg
Structure name
crystal structure of human s-adenosyl homocysteine hydrolase-like 1 protein
Structure deposition date
2010-04-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
80
Peptide accession
O43865
Residue number A
292
Residue number B
293
Peptide name
S-adenosylhomocysteine hydrolase-like protein 1
Ligandability
Cysteine 292 of S-adenosylhomocysteine hydrolase-like protein 1
Cysteine 293 of S-adenosylhomocysteine hydrolase-like protein 1
3mtg A 106 A 211
A redox-regulated disulphide may form within S-adenosylhomocysteine hydrolase-like protein 1 between cysteines 106 and 211. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
3mtg
Structure name
crystal structure of human s-adenosyl homocysteine hydrolase-like 1 protein
Structure deposition date
2010-04-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
48
Peptide accession
O43865
Residue number A
106
Residue number B
211
Peptide name
S-adenosylhomocysteine hydrolase-like protein 1
Ligandability
Cysteine 106 of S-adenosylhomocysteine hydrolase-like protein 1
Cysteine 211 of S-adenosylhomocysteine hydrolase-like protein 1
3mtg A 326 A 327
A redox-regulated disulphide may form within S-adenosylhomocysteine hydrolase-like protein 1 between cysteines 326 and 327. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
3mtg
Structure name
crystal structure of human s-adenosyl homocysteine hydrolase-like 1 protein
Structure deposition date
2010-04-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
87
Minimum pKa ?
13
% buried
100
Peptide accession
O43865
Residue number A
326
Residue number B
327
Peptide name
S-adenosylhomocysteine hydrolase-like protein 1
Ligandability
Cysteine 326 of S-adenosylhomocysteine hydrolase-like protein 1
Cysteine 327 of S-adenosylhomocysteine hydrolase-like protein 1
3mtg A 326 A 373
A redox-regulated disulphide may form within S-adenosylhomocysteine hydrolase-like protein 1 between cysteines 326 and 373. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
3mtg
Structure name
crystal structure of human s-adenosyl homocysteine hydrolase-like 1 protein
Structure deposition date
2010-04-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
88
Minimum pKa ?
13
% buried
100
Peptide accession
O43865
Residue number A
326
Residue number B
373
Peptide name
S-adenosylhomocysteine hydrolase-like protein 1
Ligandability
Cysteine 326 of S-adenosylhomocysteine hydrolase-like protein 1
Cysteine 373 of S-adenosylhomocysteine hydrolase-like protein 1
3mtg A 151 A 177
A redox-regulated disulphide may form within S-adenosylhomocysteine hydrolase-like protein 1 between cysteines 151 and 177. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
3mtg
Structure name
crystal structure of human s-adenosyl homocysteine hydrolase-like 1 protein
Structure deposition date
2010-04-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
85
Minimum pKa ?
15
% buried
94
Peptide accession
O43865
Residue number A
151
Residue number B
177
Peptide name
S-adenosylhomocysteine hydrolase-like protein 1
Ligandability
Cysteine 151 of S-adenosylhomocysteine hydrolase-like protein 1
Cysteine 177 of S-adenosylhomocysteine hydrolase-like protein 1
3mtg B 151 B 215
A redox-regulated disulphide may form within S-adenosylhomocysteine hydrolase-like protein 1 between cysteines 151 and 215. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
3mtg
Structure name
crystal structure of human s-adenosyl homocysteine hydrolase-like 1 protein
Structure deposition date
2010-04-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
100
Peptide accession
O43865
Residue number A
151
Residue number B
215
Peptide name
S-adenosylhomocysteine hydrolase-like protein 1
Ligandability
Cysteine 151 of S-adenosylhomocysteine hydrolase-like protein 1
Cysteine 215 of S-adenosylhomocysteine hydrolase-like protein 1
3mtg A 327 A 373
A redox-regulated disulphide may form within S-adenosylhomocysteine hydrolase-like protein 1 between cysteines 327 and 373. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
3mtg
Structure name
crystal structure of human s-adenosyl homocysteine hydrolase-like 1 protein
Structure deposition date
2010-04-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
14
% buried
100
Peptide accession
O43865
Residue number A
327
Residue number B
373
Peptide name
S-adenosylhomocysteine hydrolase-like protein 1
Ligandability
Cysteine 327 of S-adenosylhomocysteine hydrolase-like protein 1
Cysteine 373 of S-adenosylhomocysteine hydrolase-like protein 1
3mtg B 317 B 373
A redox-regulated disulphide may form within S-adenosylhomocysteine hydrolase-like protein 1 between cysteines 317 and 373. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
3mtg
Structure name
crystal structure of human s-adenosyl homocysteine hydrolase-like 1 protein
Structure deposition date
2010-04-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
94
Minimum pKa ?
12
% buried
100
Peptide accession
O43865
Residue number A
317
Residue number B
373
Peptide name
S-adenosylhomocysteine hydrolase-like protein 1
Ligandability
Cysteine 317 of S-adenosylhomocysteine hydrolase-like protein 1
Cysteine 373 of S-adenosylhomocysteine hydrolase-like protein 1
3mtg A 326 A 395
A redox-regulated disulphide may form within S-adenosylhomocysteine hydrolase-like protein 1 between cysteines 326 and 395. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
3mtg
Structure name
crystal structure of human s-adenosyl homocysteine hydrolase-like 1 protein
Structure deposition date
2010-04-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
92
Minimum pKa ?
12
% buried
100
Peptide accession
O43865
Residue number A
326
Residue number B
395
Peptide name
S-adenosylhomocysteine hydrolase-like protein 1
Ligandability
Cysteine 326 of S-adenosylhomocysteine hydrolase-like protein 1
Cysteine 395 of S-adenosylhomocysteine hydrolase-like protein 1
3mtg B 211 B 215
A redox-regulated disulphide may form within S-adenosylhomocysteine hydrolase-like protein 1 between cysteines 211 and 215. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
3mtg
Structure name
crystal structure of human s-adenosyl homocysteine hydrolase-like 1 protein
Structure deposition date
2010-04-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
83
Peptide accession
O43865
Residue number A
211
Residue number B
215
Peptide name
S-adenosylhomocysteine hydrolase-like protein 1
Ligandability
Cysteine 211 of S-adenosylhomocysteine hydrolase-like protein 1
Cysteine 215 of S-adenosylhomocysteine hydrolase-like protein 1
3mtg A 293 A 326
A redox-regulated disulphide may form within S-adenosylhomocysteine hydrolase-like protein 1 between cysteines 293 and 326. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
3mtg
Structure name
crystal structure of human s-adenosyl homocysteine hydrolase-like 1 protein
Structure deposition date
2010-04-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
13
% buried
94
Peptide accession
O43865
Residue number A
293
Residue number B
326
Peptide name
S-adenosylhomocysteine hydrolase-like protein 1
Ligandability
Cysteine 293 of S-adenosylhomocysteine hydrolase-like protein 1
Cysteine 326 of S-adenosylhomocysteine hydrolase-like protein 1
3mtg B 172 B 215
A redox-regulated disulphide may form within S-adenosylhomocysteine hydrolase-like protein 1 between cysteines 172 and 215. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
3mtg
Structure name
crystal structure of human s-adenosyl homocysteine hydrolase-like 1 protein
Structure deposition date
2010-04-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
96
Peptide accession
O43865
Residue number A
172
Residue number B
215
Peptide name
S-adenosylhomocysteine hydrolase-like protein 1
Ligandability
Cysteine 172 of S-adenosylhomocysteine hydrolase-like protein 1
Cysteine 215 of S-adenosylhomocysteine hydrolase-like protein 1
3mtg B 373 B 395
A redox-regulated disulphide may form within S-adenosylhomocysteine hydrolase-like protein 1 between cysteines 373 and 395. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
28
PDB code
3mtg
Structure name
crystal structure of human s-adenosyl homocysteine hydrolase-like 1 protein
Structure deposition date
2010-04-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
91
Minimum pKa ?
12
% buried
100
Peptide accession
O43865
Residue number A
373
Residue number B
395
Peptide name
S-adenosylhomocysteine hydrolase-like protein 1
Ligandability
Cysteine 373 of S-adenosylhomocysteine hydrolase-like protein 1
Cysteine 395 of S-adenosylhomocysteine hydrolase-like protein 1
3mtg A 293 A 373
A redox-regulated disulphide may form within S-adenosylhomocysteine hydrolase-like protein 1 between cysteines 293 and 373. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
27
PDB code
3mtg
Structure name
crystal structure of human s-adenosyl homocysteine hydrolase-like 1 protein
Structure deposition date
2010-04-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
14
% buried
94
Peptide accession
O43865
Residue number A
293
Residue number B
373
Peptide name
S-adenosylhomocysteine hydrolase-like protein 1
Ligandability
Cysteine 293 of S-adenosylhomocysteine hydrolase-like protein 1
Cysteine 373 of S-adenosylhomocysteine hydrolase-like protein 1
3mtg A 317 A 327
A redox-regulated disulphide may form within S-adenosylhomocysteine hydrolase-like protein 1 between cysteines 317 and 327. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
27
PDB code
3mtg
Structure name
crystal structure of human s-adenosyl homocysteine hydrolase-like 1 protein
Structure deposition date
2010-04-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
93
Minimum pKa ?
11
% buried
100
Peptide accession
O43865
Residue number A
317
Residue number B
327
Peptide name
S-adenosylhomocysteine hydrolase-like protein 1
Ligandability
Cysteine 317 of S-adenosylhomocysteine hydrolase-like protein 1
Cysteine 327 of S-adenosylhomocysteine hydrolase-like protein 1
3mtg A 151 A 211
A redox-regulated disulphide may form within S-adenosylhomocysteine hydrolase-like protein 1 between cysteines 151 and 211. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
26
PDB code
3mtg
Structure name
crystal structure of human s-adenosyl homocysteine hydrolase-like 1 protein
Structure deposition date
2010-04-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
84
Minimum pKa ?
13
% buried
82
Peptide accession
O43865
Residue number A
151
Residue number B
211
Peptide name
S-adenosylhomocysteine hydrolase-like protein 1
Ligandability
Cysteine 151 of S-adenosylhomocysteine hydrolase-like protein 1
Cysteine 211 of S-adenosylhomocysteine hydrolase-like protein 1
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