Arylsulfatase A
Intermolecular
Cysteine 341 of Formylglycine-generating enzyme and cysteine 69
Intramolecular
Cysteine 493 and cysteine 499
Cysteine 161 and cysteine 168
Cysteine 488 and cysteine 500
Cysteine 156 and cysteine 172
Cysteine 489 and cysteine 502
Cysteine 300 and cysteine 414
Cysteine 493 and cysteine 500
Cysteine 488 and cysteine 493
Cysteine 499 and cysteine 500
More...Cysteine 156 and cysteine 168
Cysteine 488 and cysteine 499
Cysteine 168 and cysteine 172
Cysteine 156 and cysteine 161
Cysteine 161 and cysteine 172
Cysteine 488 and cysteine 489
Cysteine 489 and cysteine 500
Cysteine 489 and cysteine 493
Cysteine 488 and cysteine 502
Cysteine 500 and cysteine 502
Cysteine 493 and cysteine 502
2aij X 341 P 69
A redox-regulated disulphide may form between cysteine 341 of Formylglycine-generating enzyme and cysteine 69 of Arylsulfatase A.
Details
Redox score ?
90
PDB code
2aij
Structure name
formylglycine generating enzyme c336s mutant covalently bound to substrate peptide ctpsr
Structure deposition date
2005-07-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
Formylglycine-generating enzyme
Peptide B name
Arylsulfatase A
Peptide A accession
Q8NBK3
Peptide B accession
P15289
Peptide A residue number
341
Peptide B residue number
69
Ligandability
Cysteine 341 of Formylglycine-generating enzyme
Cysteine 69 of Arylsulfatase A
1e33 P 493 P 499
A redox-regulated disulphide may form within Arylsulfatase A between cysteines 493 and 499.
Details
Redox score ?
87
PDB code
1e33
Structure name
crystal structure of an arylsulfatase a mutant p426l
Structure deposition date
2000-06-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
36
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15289
Residue number A
493
Residue number B
499
Peptide name
Arylsulfatase A
Ligandability
Cysteine 493 of Arylsulfatase A
Cysteine 499 of Arylsulfatase A
1e3c P 161 P 168
A redox-regulated disulphide may form within Arylsulfatase A between cysteines 161 and 168.
Details
Redox score ?
85
PDB code
1e3c
Structure name
crystal structure of an arylsulfatase a mutant c69s soaked in synthetic substrate
Structure deposition date
2000-06-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15289
Residue number A
161
Residue number B
168
Peptide name
Arylsulfatase A
Ligandability
Cysteine 161 of Arylsulfatase A
Cysteine 168 of Arylsulfatase A
1n2k A 488 A 500
A redox-regulated disulphide may form within Arylsulfatase A between cysteines 488 and 500.
Details
Redox score ?
85
PDB code
1n2k
Structure name
crystal structure of a covalent intermediate of endogenous human arylsulfatase a
Structure deposition date
2002-10-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15289
Residue number A
488
Residue number B
500
Peptide name
Arylsulfatase A
Ligandability
Cysteine 488 of Arylsulfatase A
Cysteine 500 of Arylsulfatase A
1n2l A 156 A 172
A redox-regulated disulphide may form within Arylsulfatase A between cysteines 156 and 172.
Details
Redox score ?
85
PDB code
1n2l
Structure name
crystal structure of a covalent intermediate of endogenous human arylsulfatase a
Structure deposition date
2002-10-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15289
Residue number A
156
Residue number B
172
Peptide name
Arylsulfatase A
Ligandability
Cysteine 156 of Arylsulfatase A
Cysteine 172 of Arylsulfatase A
1n2k A 489 A 502
A redox-regulated disulphide may form within Arylsulfatase A between cysteines 489 and 502.
Details
Redox score ?
83
PDB code
1n2k
Structure name
crystal structure of a covalent intermediate of endogenous human arylsulfatase a
Structure deposition date
2002-10-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15289
Residue number A
489
Residue number B
502
Peptide name
Arylsulfatase A
Ligandability
Cysteine 489 of Arylsulfatase A
Cysteine 502 of Arylsulfatase A
1e33 P 300 P 414
A redox-regulated disulphide may form within Arylsulfatase A between cysteines 300 and 414.
Details
Redox score ?
79
PDB code
1e33
Structure name
crystal structure of an arylsulfatase a mutant p426l
Structure deposition date
2000-06-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15289
Residue number A
300
Residue number B
414
Peptide name
Arylsulfatase A
Ligandability
Cysteine 300 of Arylsulfatase A
Cysteine 414 of Arylsulfatase A
1auk A 493 A 500
A redox-regulated disulphide may form within Arylsulfatase A between cysteines 493 and 500.
Details
Redox score ?
78
PDB code
1auk
Structure name
human arylsulfatase a
Structure deposition date
1997-08-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15289
Residue number A
493
Residue number B
500
Peptide name
Arylsulfatase A
Ligandability
Cysteine 493 of Arylsulfatase A
Cysteine 500 of Arylsulfatase A
1e1z P 488 P 493
A redox-regulated disulphide may form within Arylsulfatase A between cysteines 488 and 493.
Details
Redox score ?
76
PDB code
1e1z
Structure name
crystal structure of an arylsulfatase a mutant c69s
Structure deposition date
2000-05-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15289
Residue number A
488
Residue number B
493
Peptide name
Arylsulfatase A
Ligandability
Cysteine 488 of Arylsulfatase A
Cysteine 493 of Arylsulfatase A
1n2k A 499 A 500
A redox-regulated disulphide may form within Arylsulfatase A between cysteines 499 and 500.
Details
Redox score ?
71
PDB code
1n2k
Structure name
crystal structure of a covalent intermediate of endogenous human arylsulfatase a
Structure deposition date
2002-10-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15289
Residue number A
499
Residue number B
500
Peptide name
Arylsulfatase A
Ligandability
Cysteine 499 of Arylsulfatase A
Cysteine 500 of Arylsulfatase A
1n2l A 156 A 168
A redox-regulated disulphide may form within Arylsulfatase A between cysteines 156 and 168.
Details
Redox score ?
70
PDB code
1n2l
Structure name
crystal structure of a covalent intermediate of endogenous human arylsulfatase a
Structure deposition date
2002-10-23
Thiol separation (Å)
5
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15289
Residue number A
156
Residue number B
168
Peptide name
Arylsulfatase A
Ligandability
Cysteine 156 of Arylsulfatase A
Cysteine 168 of Arylsulfatase A
1e1z P 488 P 499
A redox-regulated disulphide may form within Arylsulfatase A between cysteines 488 and 499.
Details
Redox score ?
65
PDB code
1e1z
Structure name
crystal structure of an arylsulfatase a mutant c69s
Structure deposition date
2000-05-12
Thiol separation (Å)
5
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15289
Residue number A
488
Residue number B
499
Peptide name
Arylsulfatase A
Ligandability
Cysteine 488 of Arylsulfatase A
Cysteine 499 of Arylsulfatase A
1e1z P 168 P 172
A redox-regulated disulphide may form within Arylsulfatase A between cysteines 168 and 172.
Details
Redox score ?
63
PDB code
1e1z
Structure name
crystal structure of an arylsulfatase a mutant c69s
Structure deposition date
2000-05-12
Thiol separation (Å)
6
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15289
Residue number A
168
Residue number B
172
Peptide name
Arylsulfatase A
Ligandability
Cysteine 168 of Arylsulfatase A
Cysteine 172 of Arylsulfatase A
1n2l A 156 A 161
A redox-regulated disulphide may form within Arylsulfatase A between cysteines 156 and 161. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
60
PDB code
1n2l
Structure name
crystal structure of a covalent intermediate of endogenous human arylsulfatase a
Structure deposition date
2002-10-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15289
Residue number A
156
Residue number B
161
Peptide name
Arylsulfatase A
Ligandability
Cysteine 156 of Arylsulfatase A
Cysteine 161 of Arylsulfatase A
1n2k A 161 A 172
A redox-regulated disulphide may form within Arylsulfatase A between cysteines 161 and 172. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
1n2k
Structure name
crystal structure of a covalent intermediate of endogenous human arylsulfatase a
Structure deposition date
2002-10-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15289
Residue number A
161
Residue number B
172
Peptide name
Arylsulfatase A
Ligandability
Cysteine 161 of Arylsulfatase A
Cysteine 172 of Arylsulfatase A
1e3c P 488 P 489
A redox-regulated disulphide may form within Arylsulfatase A between cysteines 488 and 489. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
1e3c
Structure name
crystal structure of an arylsulfatase a mutant c69s soaked in synthetic substrate
Structure deposition date
2000-06-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15289
Residue number A
488
Residue number B
489
Peptide name
Arylsulfatase A
Ligandability
Cysteine 488 of Arylsulfatase A
Cysteine 489 of Arylsulfatase A
1e33 P 489 P 500
A redox-regulated disulphide may form within Arylsulfatase A between cysteines 489 and 500. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
1e33
Structure name
crystal structure of an arylsulfatase a mutant p426l
Structure deposition date
2000-06-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15289
Residue number A
489
Residue number B
500
Peptide name
Arylsulfatase A
Ligandability
Cysteine 489 of Arylsulfatase A
Cysteine 500 of Arylsulfatase A
1e1z P 489 P 493
A redox-regulated disulphide may form within Arylsulfatase A between cysteines 489 and 493. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
1e1z
Structure name
crystal structure of an arylsulfatase a mutant c69s
Structure deposition date
2000-05-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15289
Residue number A
489
Residue number B
493
Peptide name
Arylsulfatase A
Ligandability
Cysteine 489 of Arylsulfatase A
Cysteine 493 of Arylsulfatase A
1n2k A 488 A 502
A redox-regulated disulphide may form within Arylsulfatase A between cysteines 488 and 502. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
1n2k
Structure name
crystal structure of a covalent intermediate of endogenous human arylsulfatase a
Structure deposition date
2002-10-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15289
Residue number A
488
Residue number B
502
Peptide name
Arylsulfatase A
Ligandability
Cysteine 488 of Arylsulfatase A
Cysteine 502 of Arylsulfatase A
1e2s P 500 P 502
A redox-regulated disulphide may form within Arylsulfatase A between cysteines 500 and 502. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
1e2s
Structure name
crystal structure of an arylsulfatase a mutant c69a
Structure deposition date
2000-05-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15289
Residue number A
500
Residue number B
502
Peptide name
Arylsulfatase A
Ligandability
Cysteine 500 of Arylsulfatase A
Cysteine 502 of Arylsulfatase A
1n2k A 493 A 502
A redox-regulated disulphide may form within Arylsulfatase A between cysteines 493 and 502. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
1n2k
Structure name
crystal structure of a covalent intermediate of endogenous human arylsulfatase a
Structure deposition date
2002-10-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
40
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15289
Residue number A
493
Residue number B
502
Peptide name
Arylsulfatase A
Ligandability
Cysteine 493 of Arylsulfatase A
Cysteine 502 of Arylsulfatase A
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