Ubiquitin carboxyl-terminal hydrolase 21
Intramolecular
Cysteine 437 and cysteine 440
Cysteine 384 and cysteine 437
Cysteine 387 and cysteine 437
Cysteine 384 and cysteine 440
Cysteine 384 and cysteine 387
Cysteine 387 and cysteine 440
Cysteine 229 and cysteine 523
Cysteine 229 and cysteine 508
Cysteine 523 and cysteine 525
Cysteine 508 and cysteine 523
Cysteine 221 and cysteine 508
3i3t E 437 E 440
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 21 between cysteines 437 and 440.
Details
Redox score ?
91
PDB code
3i3t
Structure name
crystal structure of covalent ubiquitin-usp21 complex
Structure deposition date
2009-06-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
46
Minimum pKa ?
6
% buried
1
Peptide accession
Q9UK80
Residue number A
437
Residue number B
440
Peptide name
Ubiquitin carboxyl-terminal hydrolase 21
Ligandability
Cysteine 437 of Ubiquitin carboxyl-terminal hydrolase 21
Cysteine 440 of Ubiquitin carboxyl-terminal hydrolase 21
3mtn C 384 C 437
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 21 between cysteines 384 and 437.
Details
Redox score ?
90
PDB code
3mtn
Structure name
usp21 in complex with a ubiquitin-based, usp21-specific inhibitor
Structure deposition date
2010-04-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
58
Minimum pKa ?
6
% buried
6
Peptide accession
Q9UK80
Residue number A
384
Residue number B
437
Peptide name
Ubiquitin carboxyl-terminal hydrolase 21
Ligandability
Cysteine 384 of Ubiquitin carboxyl-terminal hydrolase 21
Cysteine 437 of Ubiquitin carboxyl-terminal hydrolase 21
3i3t C 387 C 437
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 21 between cysteines 387 and 437.
Details
Redox score ?
90
PDB code
3i3t
Structure name
crystal structure of covalent ubiquitin-usp21 complex
Structure deposition date
2009-06-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
47
Minimum pKa ?
6
% buried
0
Peptide accession
Q9UK80
Residue number A
387
Residue number B
437
Peptide name
Ubiquitin carboxyl-terminal hydrolase 21
Ligandability
Cysteine 387 of Ubiquitin carboxyl-terminal hydrolase 21
Cysteine 437 of Ubiquitin carboxyl-terminal hydrolase 21
3mtn C 384 C 440
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 21 between cysteines 384 and 440.
Details
Redox score ?
82
PDB code
3mtn
Structure name
usp21 in complex with a ubiquitin-based, usp21-specific inhibitor
Structure deposition date
2010-04-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
3
Peptide accession
Q9UK80
Residue number A
384
Residue number B
440
Peptide name
Ubiquitin carboxyl-terminal hydrolase 21
Ligandability
Cysteine 384 of Ubiquitin carboxyl-terminal hydrolase 21
Cysteine 440 of Ubiquitin carboxyl-terminal hydrolase 21
3i3t C 384 C 387
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 21 between cysteines 384 and 387.
Details
Redox score ?
80
PDB code
3i3t
Structure name
crystal structure of covalent ubiquitin-usp21 complex
Structure deposition date
2009-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
7
% buried
1
Peptide accession
Q9UK80
Residue number A
384
Residue number B
387
Peptide name
Ubiquitin carboxyl-terminal hydrolase 21
Ligandability
Cysteine 384 of Ubiquitin carboxyl-terminal hydrolase 21
Cysteine 387 of Ubiquitin carboxyl-terminal hydrolase 21
3mtn C 387 C 440
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 21 between cysteines 387 and 440.
Details
Redox score ?
79
PDB code
3mtn
Structure name
usp21 in complex with a ubiquitin-based, usp21-specific inhibitor
Structure deposition date
2010-04-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
8
% buried
0
Peptide accession
Q9UK80
Residue number A
387
Residue number B
440
Peptide name
Ubiquitin carboxyl-terminal hydrolase 21
Ligandability
Cysteine 387 of Ubiquitin carboxyl-terminal hydrolase 21
Cysteine 440 of Ubiquitin carboxyl-terminal hydrolase 21
3i3t G 229 G 523
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 21 between cysteines 229 and 523.
Details
Redox score ?
67
PDB code
3i3t
Structure name
crystal structure of covalent ubiquitin-usp21 complex
Structure deposition date
2009-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
88
Minimum pKa ?
8
% buried
100
Peptide accession
Q9UK80
Residue number A
229
Residue number B
523
Peptide name
Ubiquitin carboxyl-terminal hydrolase 21
Ligandability
Cysteine 229 of Ubiquitin carboxyl-terminal hydrolase 21
Cysteine 523 of Ubiquitin carboxyl-terminal hydrolase 21
3i3t A 229 A 508
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 21 between cysteines 229 and 508.
Details
Redox score ?
64
PDB code
3i3t
Structure name
crystal structure of covalent ubiquitin-usp21 complex
Structure deposition date
2009-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
89
Minimum pKa ?
9
% buried
100
Peptide accession
Q9UK80
Residue number A
229
Residue number B
508
Peptide name
Ubiquitin carboxyl-terminal hydrolase 21
Ligandability
Cysteine 229 of Ubiquitin carboxyl-terminal hydrolase 21
Cysteine 508 of Ubiquitin carboxyl-terminal hydrolase 21
3i3t A 523 A 525
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 21 between cysteines 523 and 525. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
3i3t
Structure name
crystal structure of covalent ubiquitin-usp21 complex
Structure deposition date
2009-06-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
8
% buried
62
Peptide accession
Q9UK80
Residue number A
523
Residue number B
525
Peptide name
Ubiquitin carboxyl-terminal hydrolase 21
Ligandability
Cysteine 523 of Ubiquitin carboxyl-terminal hydrolase 21
Cysteine 525 of Ubiquitin carboxyl-terminal hydrolase 21
3mtn A 508 A 523
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 21 between cysteines 508 and 523. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
3mtn
Structure name
usp21 in complex with a ubiquitin-based, usp21-specific inhibitor
Structure deposition date
2010-04-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
94
Minimum pKa ?
8
% buried
100
Peptide accession
Q9UK80
Residue number A
508
Residue number B
523
Peptide name
Ubiquitin carboxyl-terminal hydrolase 21
Ligandability
Cysteine 508 of Ubiquitin carboxyl-terminal hydrolase 21
Cysteine 523 of Ubiquitin carboxyl-terminal hydrolase 21
3i3t E 221 E 508
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 21 between cysteines 221 and 508. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
3i3t
Structure name
crystal structure of covalent ubiquitin-usp21 complex
Structure deposition date
2009-06-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
91
Minimum pKa ?
9
% buried
100
Peptide accession
Q9UK80
Residue number A
221
Residue number B
508
Peptide name
Ubiquitin carboxyl-terminal hydrolase 21
Ligandability
Cysteine 221 of Ubiquitin carboxyl-terminal hydrolase 21
Cysteine 508 of Ubiquitin carboxyl-terminal hydrolase 21
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