Ubiquitin-associated and SH3 domain-containing protein B
Intramolecular
Cysteine 611 and cysteine 613
Cysteine 468 and cysteine 474
Cysteine 374 and cysteine 602
Cysteine 583 and cysteine 611
Cysteine 574 and cysteine 602
Cysteine 385 and cysteine 611
Cysteine 572 and cysteine 602
Cysteine 389 and cysteine 474
Cysteine 389 and cysteine 611
5w5g A 600 A 602
A redox-regulated disulphide may form within Ubiquitin-associated and SH3 domain-containing protein B between cysteines 611 and 613 (600 and 602 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
5w5g
Structure name
structure of human sts-1 histidine phosphatase domain
Structure deposition date
2017-06-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
78
Peptide accession
Q8TF42
Residue number A
611
Residue number B
613
Peptide name
Ubiquitin-associated and SH3 domain-containing protein B
Ligandability
Cysteine 611 of Ubiquitin-associated and SH3 domain-containing protein B
Cysteine 613 of Ubiquitin-associated and SH3 domain-containing protein B
5vr6 A 457 A 463
A redox-regulated disulphide may form within Ubiquitin-associated and SH3 domain-containing protein B between cysteines 468 and 474 (457 and 463 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
5vr6
Structure name
structure of human sts-1 histidine phosphatase domain with sulfate bound
Structure deposition date
2017-05-10
Thiol separation (Å)
6
Half-sphere exposure sum ?
98
Minimum pKa ?
12
% buried
100
Peptide accession
Q8TF42
Residue number A
468
Residue number B
474
Peptide name
Ubiquitin-associated and SH3 domain-containing protein B
Ligandability
Cysteine 468 of Ubiquitin-associated and SH3 domain-containing protein B
Cysteine 474 of Ubiquitin-associated and SH3 domain-containing protein B
2ikq B 374 B 602
A redox-regulated disulphide may form within Ubiquitin-associated and SH3 domain-containing protein B between cysteines 374 and 602. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
2ikq
Structure name
crystal structure of mouse sts-1 pgm domain in complex with phosphate
Structure deposition date
2006-10-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
10
% buried
56
Peptide accession
Q8BGG7
Residue number A
374
Residue number B
602
Peptide name
Ubiquitin-associated and SH3 domain-containing protein B
Ligandability
Cysteine 374 of Ubiquitin-associated and SH3 domain-containing protein B
Cysteine 602 of Ubiquitin-associated and SH3 domain-containing protein B
5vr6 A 572 A 600
A redox-regulated disulphide may form within Ubiquitin-associated and SH3 domain-containing protein B between cysteines 583 and 611 (572 and 600 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
5vr6
Structure name
structure of human sts-1 histidine phosphatase domain with sulfate bound
Structure deposition date
2017-05-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
94
Minimum pKa ?
11
% buried
100
Peptide accession
Q8TF42
Residue number A
583
Residue number B
611
Peptide name
Ubiquitin-associated and SH3 domain-containing protein B
Ligandability
Cysteine 583 of Ubiquitin-associated and SH3 domain-containing protein B
Cysteine 611 of Ubiquitin-associated and SH3 domain-containing protein B
3mbk A 574 A 602
A redox-regulated disulphide may form within Ubiquitin-associated and SH3 domain-containing protein B between cysteines 574 and 602. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
3mbk
Structure name
the 1
Structure deposition date
2010-03-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
44
Peptide accession
Q8BGG7
Residue number A
574
Residue number B
602
Peptide name
Ubiquitin-associated and SH3 domain-containing protein B
Ligandability
Cysteine 574 of Ubiquitin-associated and SH3 domain-containing protein B
Cysteine 602 of Ubiquitin-associated and SH3 domain-containing protein B
5vr6 B 374 B 600
A redox-regulated disulphide may form within Ubiquitin-associated and SH3 domain-containing protein B between cysteines 385 and 611 (374 and 600 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
5vr6
Structure name
structure of human sts-1 histidine phosphatase domain with sulfate bound
Structure deposition date
2017-05-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
10
% buried
80
Peptide accession
Q8TF42
Residue number A
385
Residue number B
611
Peptide name
Ubiquitin-associated and SH3 domain-containing protein B
Ligandability
Cysteine 385 of Ubiquitin-associated and SH3 domain-containing protein B
Cysteine 611 of Ubiquitin-associated and SH3 domain-containing protein B
2ikq A 572 A 602
A redox-regulated disulphide may form within Ubiquitin-associated and SH3 domain-containing protein B between cysteines 572 and 602. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
2ikq
Structure name
crystal structure of mouse sts-1 pgm domain in complex with phosphate
Structure deposition date
2006-10-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
11
% buried
82
Peptide accession
Q8BGG7
Residue number A
572
Residue number B
602
Peptide name
Ubiquitin-associated and SH3 domain-containing protein B
Ligandability
Cysteine 572 of Ubiquitin-associated and SH3 domain-containing protein B
Cysteine 602 of Ubiquitin-associated and SH3 domain-containing protein B
5w5g B 378 B 463
A redox-regulated disulphide may form within Ubiquitin-associated and SH3 domain-containing protein B between cysteines 389 and 474 (378 and 463 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
5w5g
Structure name
structure of human sts-1 histidine phosphatase domain
Structure deposition date
2017-06-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
96
Minimum pKa ?
12
% buried
100
Peptide accession
Q8TF42
Residue number A
389
Residue number B
474
Peptide name
Ubiquitin-associated and SH3 domain-containing protein B
Ligandability
Cysteine 389 of Ubiquitin-associated and SH3 domain-containing protein B
Cysteine 474 of Ubiquitin-associated and SH3 domain-containing protein B
5w5g A 378 A 600
A redox-regulated disulphide may form within Ubiquitin-associated and SH3 domain-containing protein B between cysteines 389 and 611 (378 and 600 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
5w5g
Structure name
structure of human sts-1 histidine phosphatase domain
Structure deposition date
2017-06-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
98
Peptide accession
Q8TF42
Residue number A
389
Residue number B
611
Peptide name
Ubiquitin-associated and SH3 domain-containing protein B
Ligandability
Cysteine 389 of Ubiquitin-associated and SH3 domain-containing protein B
Cysteine 611 of Ubiquitin-associated and SH3 domain-containing protein B
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