Aromatic-L-amino-acid decarboxylase
Intramolecular
Cysteine 410 and cysteine 438
Cysteine 100 and cysteine 111
Cysteine 248 and cysteine 438
Cysteine 248 and cysteine 410
Cysteine 95 and cysteine 100
Cysteine 401 and cysteine 410
Cysteine 248 and cysteine 249
Cysteine 95 and cysteine 111
Cysteine 401 and cysteine 438
Cysteine 248 and cysteine 401
More...Cysteine 249 and cysteine 410
Cysteine 249 and cysteine 451
3rch A 410 A 438
A redox-regulated disulphide may form within Aromatic-L-amino-acid decarboxylase between cysteines 410 and 438.
Details
Redox score ?
67
PDB code
3rch
Structure name
crystal structure of human aromatic l-amino acid decarboxylase (aadc) in the open conformation with llp and plp bound to chain-a and chain- b respectively
Structure deposition date
2011-03-31
Thiol separation (Å)
5
Half-sphere exposure sum ?
71
Minimum pKa ?
7
% buried
87
Peptide accession
P20711
Residue number A
410
Residue number B
438
Peptide name
Aromatic-L-amino-acid decarboxylase
Ligandability
Cysteine 410 of Aromatic-L-amino-acid decarboxylase
Cysteine 438 of Aromatic-L-amino-acid decarboxylase
1js6 A 100 A 111
A redox-regulated disulphide may form within Aromatic-L-amino-acid decarboxylase between cysteines 100 and 111.
Details
Redox score ?
64
PDB code
1js6
Structure name
crystal structure of dopa decarboxylase
Structure deposition date
2001-08-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
92
Minimum pKa ?
9
% buried
100
Peptide accession
P80041
Residue number A
100
Residue number B
111
Peptide name
Aromatic-L-amino-acid decarboxylase
Ligandability
Cysteine 100 of Aromatic-L-amino-acid decarboxylase
Cysteine 111 of Aromatic-L-amino-acid decarboxylase
3rch A 248 A 438
A redox-regulated disulphide may form within Aromatic-L-amino-acid decarboxylase between cysteines 248 and 438. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
3rch
Structure name
crystal structure of human aromatic l-amino acid decarboxylase (aadc) in the open conformation with llp and plp bound to chain-a and chain- b respectively
Structure deposition date
2011-03-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
7
% buried
78
Peptide accession
P20711
Residue number A
248
Residue number B
438
Peptide name
Aromatic-L-amino-acid decarboxylase
Ligandability
Cysteine 248 of Aromatic-L-amino-acid decarboxylase
Cysteine 438 of Aromatic-L-amino-acid decarboxylase
3rbl B 248 B 410
A redox-regulated disulphide may form within Aromatic-L-amino-acid decarboxylase between cysteines 248 and 410. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
3rbl
Structure name
crystal structure of human aromatic l-amino acid decarboxylase (aadc) in the apo form
Structure deposition date
2011-03-29
Thiol separation (Å)
5
Half-sphere exposure sum ?
86
Minimum pKa ?
11
% buried
85
Peptide accession
P20711
Residue number A
248
Residue number B
410
Peptide name
Aromatic-L-amino-acid decarboxylase
Ligandability
Cysteine 248 of Aromatic-L-amino-acid decarboxylase
Cysteine 410 of Aromatic-L-amino-acid decarboxylase
1js3 B 95 B 100
A redox-regulated disulphide may form within Aromatic-L-amino-acid decarboxylase between cysteines 95 and 100. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
1js3
Structure name
crystal structure of dopa decarboxylase in complex with the inhibitor carbidopa
Structure deposition date
2001-08-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
88
Minimum pKa ?
9
% buried
100
Peptide accession
P80041
Residue number A
95
Residue number B
100
Peptide name
Aromatic-L-amino-acid decarboxylase
Ligandability
Cysteine 95 of Aromatic-L-amino-acid decarboxylase
Cysteine 100 of Aromatic-L-amino-acid decarboxylase
3rbl B 401 B 410
A redox-regulated disulphide may form within Aromatic-L-amino-acid decarboxylase between cysteines 401 and 410. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
3rbl
Structure name
crystal structure of human aromatic l-amino acid decarboxylase (aadc) in the apo form
Structure deposition date
2011-03-29
Thiol separation (Å)
6
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
82
Peptide accession
P20711
Residue number A
401
Residue number B
410
Peptide name
Aromatic-L-amino-acid decarboxylase
Ligandability
Cysteine 401 of Aromatic-L-amino-acid decarboxylase
Cysteine 410 of Aromatic-L-amino-acid decarboxylase
3rch B 248 B 249
A redox-regulated disulphide may form within Aromatic-L-amino-acid decarboxylase between cysteines 248 and 249. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
3rch
Structure name
crystal structure of human aromatic l-amino acid decarboxylase (aadc) in the open conformation with llp and plp bound to chain-a and chain- b respectively
Structure deposition date
2011-03-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
9
% buried
90
Peptide accession
P20711
Residue number A
248
Residue number B
249
Peptide name
Aromatic-L-amino-acid decarboxylase
Ligandability
Cysteine 248 of Aromatic-L-amino-acid decarboxylase
Cysteine 249 of Aromatic-L-amino-acid decarboxylase
1js6 A 95 A 111
A redox-regulated disulphide may form within Aromatic-L-amino-acid decarboxylase between cysteines 95 and 111. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
1js6
Structure name
crystal structure of dopa decarboxylase
Structure deposition date
2001-08-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
100
Peptide accession
P80041
Residue number A
95
Residue number B
111
Peptide name
Aromatic-L-amino-acid decarboxylase
Ligandability
Cysteine 95 of Aromatic-L-amino-acid decarboxylase
Cysteine 111 of Aromatic-L-amino-acid decarboxylase
3rch B 401 B 438
A redox-regulated disulphide may form within Aromatic-L-amino-acid decarboxylase between cysteines 401 and 438. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
3rch
Structure name
crystal structure of human aromatic l-amino acid decarboxylase (aadc) in the open conformation with llp and plp bound to chain-a and chain- b respectively
Structure deposition date
2011-03-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
58
Minimum pKa ?
11
% buried
69
Peptide accession
P20711
Residue number A
401
Residue number B
438
Peptide name
Aromatic-L-amino-acid decarboxylase
Ligandability
Cysteine 401 of Aromatic-L-amino-acid decarboxylase
Cysteine 438 of Aromatic-L-amino-acid decarboxylase
3rbl B 248 B 401
A redox-regulated disulphide may form within Aromatic-L-amino-acid decarboxylase between cysteines 248 and 401. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
3rbl
Structure name
crystal structure of human aromatic l-amino acid decarboxylase (aadc) in the apo form
Structure deposition date
2011-03-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
72
Peptide accession
P20711
Residue number A
248
Residue number B
401
Peptide name
Aromatic-L-amino-acid decarboxylase
Ligandability
Cysteine 248 of Aromatic-L-amino-acid decarboxylase
Cysteine 401 of Aromatic-L-amino-acid decarboxylase
3rbl B 249 B 410
A redox-regulated disulphide may form within Aromatic-L-amino-acid decarboxylase between cysteines 249 and 410. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
3rbl
Structure name
crystal structure of human aromatic l-amino acid decarboxylase (aadc) in the apo form
Structure deposition date
2011-03-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
14
% buried
97
Peptide accession
P20711
Residue number A
249
Residue number B
410
Peptide name
Aromatic-L-amino-acid decarboxylase
Ligandability
Cysteine 249 of Aromatic-L-amino-acid decarboxylase
Cysteine 410 of Aromatic-L-amino-acid decarboxylase
3rch B 249 B 451
A redox-regulated disulphide may form within Aromatic-L-amino-acid decarboxylase between cysteines 249 and 451. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
25
PDB code
3rch
Structure name
crystal structure of human aromatic l-amino acid decarboxylase (aadc) in the open conformation with llp and plp bound to chain-a and chain- b respectively
Structure deposition date
2011-03-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
100
Peptide accession
P20711
Residue number A
249
Residue number B
451
Peptide name
Aromatic-L-amino-acid decarboxylase
Ligandability
Cysteine 249 of Aromatic-L-amino-acid decarboxylase
Cysteine 451 of Aromatic-L-amino-acid decarboxylase
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