Low molecular weight phosphotyrosine protein phosphatase
Intramolecular
Cysteine 146 and cysteine 150 L
Cysteine 146 and cysteine 149 L
Cysteine 149 and cysteine 150
Cysteine 13 and cysteine 18 L
Cysteine 13 and cysteine 146 L
Cysteine 18 and cysteine 63 L
Cysteine 63 and cysteine 146 L
Cysteine 13 and cysteine 91 L
Cysteine 18 and cysteine 146 L
Cysteine 91 and cysteine 149 L
Cysteine 13 and cysteine 149 L
5kql A 145 A 149
A redox-regulated disulphide may form within Low molecular weight phosphotyrosine protein phosphatase between cysteines 146 and 150 (145 and 149 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
5kql
Structure name
co-crystal structure of lmw-ptp in complex with 2-oxo-1-phenyl-2- (phenylamino)ethanesulfonic acid
Structure deposition date
2016-07-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
85
Minimum pKa ?
13
% buried
100
Peptide accession
P24666
Residue number A
146
Residue number B
150
Peptide name
Low molecular weight phosphotyrosine protein phosphatase
Ligandability
Cysteine 146 of Low molecular weight phosphotyrosine protein phosphatase
Cysteine 150 of Low molecular weight phosphotyrosine protein phosphatase
5jnr A 145 A 148
A redox-regulated disulphide may form within Low molecular weight phosphotyrosine protein phosphatase between cysteines 146 and 149 (145 and 148 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5jnr
Structure name
crystal structure of human low molecular weight protein tyrosine phosphatase (lmptp) type a
Structure deposition date
2016-04-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
85
Peptide accession
P24666
Residue number A
146
Residue number B
149
Peptide name
Low molecular weight phosphotyrosine protein phosphatase
Ligandability
Cysteine 146 of Low molecular weight phosphotyrosine protein phosphatase
Cysteine 149 of Low molecular weight phosphotyrosine protein phosphatase
5jnv A 148 A 149
A redox-regulated disulphide may form within Low molecular weight phosphotyrosine protein phosphatase between cysteines 149 and 150 (148 and 149 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5jnv
Structure name
crystal structure of bovine low molecular weight protein tyrosine phosphatase (lmptp) mutant (w49y n50e) complexed with hepes
Structure deposition date
2016-04-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
85
Peptide accession
P11064
Residue number A
149
Residue number B
150
Peptide name
Low molecular weight phosphotyrosine protein phosphatase
Ligandability
Cysteine 149 of Low molecular weight phosphotyrosine protein phosphatase
Cysteine 150 of Low molecular weight phosphotyrosine protein phosphatase
5jns A 12 A 17
A redox-regulated disulphide may form within Low molecular weight phosphotyrosine protein phosphatase between cysteines 13 and 18 (12 and 17 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5jns
Structure name
crystal structure of human low molecular weight protein tyrosine phosphatase (lmptp) type a complexed with phosphate
Structure deposition date
2016-04-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
97
Minimum pKa ?
9
% buried
84
Peptide accession
P24666
Residue number A
13
Residue number B
18
Peptide name
Low molecular weight phosphotyrosine protein phosphatase
Ligandability
Cysteine 13 of Low molecular weight phosphotyrosine protein phosphatase
Cysteine 18 of Low molecular weight phosphotyrosine protein phosphatase
5kql A 12 A 145
A redox-regulated disulphide may form within Low molecular weight phosphotyrosine protein phosphatase between cysteines 13 and 146 (12 and 145 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
5kql
Structure name
co-crystal structure of lmw-ptp in complex with 2-oxo-1-phenyl-2- (phenylamino)ethanesulfonic acid
Structure deposition date
2016-07-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
95
Minimum pKa ?
7
% buried
100
Peptide accession
P24666
Residue number A
13
Residue number B
146
Peptide name
Low molecular weight phosphotyrosine protein phosphatase
Ligandability
Cysteine 13 of Low molecular weight phosphotyrosine protein phosphatase
Cysteine 146 of Low molecular weight phosphotyrosine protein phosphatase
5kqg A 17 A 62
A redox-regulated disulphide may form within Low molecular weight phosphotyrosine protein phosphatase between cysteines 18 and 63 (17 and 62 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
5kqg
Structure name
co-crystal structure of lmw-ptp in complex with 2-(benzothiazol-2- ylamino)-2-oxo-1-phenylethanesulfonic acid
Structure deposition date
2016-07-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
70
Peptide accession
P24666
Residue number A
18
Residue number B
63
Peptide name
Low molecular weight phosphotyrosine protein phosphatase
Ligandability
Cysteine 18 of Low molecular weight phosphotyrosine protein phosphatase
Cysteine 63 of Low molecular weight phosphotyrosine protein phosphatase
7kh8 B 62 B 145
A redox-regulated disulphide may form within Low molecular weight phosphotyrosine protein phosphatase between cysteines 63 and 146 (62 and 145 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
7kh8
Structure name
human lmptp in complex with inhibitor
Structure deposition date
2020-10-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
74
Peptide accession
P24666
Residue number A
63
Residue number B
146
Peptide name
Low molecular weight phosphotyrosine protein phosphatase
Ligandability
Cysteine 63 of Low molecular weight phosphotyrosine protein phosphatase
Cysteine 146 of Low molecular weight phosphotyrosine protein phosphatase
5jnt A 12 A 90
A redox-regulated disulphide may form within Low molecular weight phosphotyrosine protein phosphatase between cysteines 13 and 91 (12 and 90 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
5jnt
Structure name
crystal structure of human low molecular weight protein tyrosine phosphatase (lmptp) type a complexed with mes
Structure deposition date
2016-04-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
97
Minimum pKa ?
6
% buried
94
Peptide accession
P24666
Residue number A
13
Residue number B
91
Peptide name
Low molecular weight phosphotyrosine protein phosphatase
Ligandability
Cysteine 13 of Low molecular weight phosphotyrosine protein phosphatase
Cysteine 91 of Low molecular weight phosphotyrosine protein phosphatase
5kqg A 17 A 145
A redox-regulated disulphide may form within Low molecular weight phosphotyrosine protein phosphatase between cysteines 18 and 146 (17 and 145 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
5kqg
Structure name
co-crystal structure of lmw-ptp in complex with 2-(benzothiazol-2- ylamino)-2-oxo-1-phenylethanesulfonic acid
Structure deposition date
2016-07-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
92
Minimum pKa ?
13
% buried
100
Peptide accession
P24666
Residue number A
18
Residue number B
146
Peptide name
Low molecular weight phosphotyrosine protein phosphatase
Ligandability
Cysteine 18 of Low molecular weight phosphotyrosine protein phosphatase
Cysteine 146 of Low molecular weight phosphotyrosine protein phosphatase
1bvh A 90 A 148
A redox-regulated disulphide may form within Low molecular weight phosphotyrosine protein phosphatase between cysteines 91 and 149 (90 and 148 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
27
PDB code
1bvh
Structure name
solution structure of a low molecular weight protein tyrosine phosphatase
Structure deposition date
1994-05-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
88
Minimum pKa ?
13
% buried
91
Peptide accession
P11064
Residue number A
91
Residue number B
149
Peptide name
Low molecular weight phosphotyrosine protein phosphatase
Ligandability
Cysteine 91 of Low molecular weight phosphotyrosine protein phosphatase
Cysteine 149 of Low molecular weight phosphotyrosine protein phosphatase
1bvh A 12 A 148
A redox-regulated disulphide may form within Low molecular weight phosphotyrosine protein phosphatase between cysteines 13 and 149 (12 and 148 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
25
PDB code
1bvh
Structure name
solution structure of a low molecular weight protein tyrosine phosphatase
Structure deposition date
1994-05-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
90
Minimum pKa ?
13
% buried
97
Peptide accession
P11064
Residue number A
13
Residue number B
149
Peptide name
Low molecular weight phosphotyrosine protein phosphatase
Ligandability
Cysteine 13 of Low molecular weight phosphotyrosine protein phosphatase
Cysteine 149 of Low molecular weight phosphotyrosine protein phosphatase
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