N-acetylgalactosamine kinase
Intramolecular
Cysteine 54 and cysteine 247
Cysteine 371 and cysteine 377
Cysteine 152 and cysteine 175
Cysteine 301 and cysteine 303
Cysteine 229 and cysteine 407
Cysteine 113 and cysteine 175
Cysteine 153 and cysteine 175
Cysteine 377 and cysteine 379
Cysteine 132 and cysteine 153
Cysteine 152 and cysteine 153
2a2d A 54 A 247
A redox-regulated disulphide may form within N-acetylgalactosamine kinase between cysteines 54 and 247.
Details
Redox score ?
70
PDB code
2a2d
Structure name
x-ray structure of human n-acetyl galactosamine kinase complexed with mn-amppnp and n-acetyl glactosamine
Structure deposition date
2005-06-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
86
Minimum pKa ?
8
% buried
100
Peptide accession
Q01415
Residue number A
54
Residue number B
247
Peptide name
N-acetylgalactosamine kinase
Ligandability
Cysteine 54 of N-acetylgalactosamine kinase
Cysteine 247 of N-acetylgalactosamine kinase
2a2d A 371 A 377
A redox-regulated disulphide may form within N-acetylgalactosamine kinase between cysteines 371 and 377.
Details
Redox score ?
66
PDB code
2a2d
Structure name
x-ray structure of human n-acetyl galactosamine kinase complexed with mn-amppnp and n-acetyl glactosamine
Structure deposition date
2005-06-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
9
% buried
100
Peptide accession
Q01415
Residue number A
371
Residue number B
377
Peptide name
N-acetylgalactosamine kinase
Ligandability
Cysteine 371 of N-acetylgalactosamine kinase
Cysteine 377 of N-acetylgalactosamine kinase
2a2c A 152 A 175
A redox-regulated disulphide may form within N-acetylgalactosamine kinase between cysteines 152 and 175.
Details
Redox score ?
61
PDB code
2a2c
Structure name
x-ray structure of human n-acetyl galactosamine kinase complexed with mg-adp and n-acetyl galactosamine 1-phosphate
Structure deposition date
2005-06-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
107
Minimum pKa ?
9
% buried
100
Peptide accession
Q01415
Residue number A
152
Residue number B
175
Peptide name
N-acetylgalactosamine kinase
Ligandability
Cysteine 152 of N-acetylgalactosamine kinase
Cysteine 175 of N-acetylgalactosamine kinase
2a2d A 301 A 303
A redox-regulated disulphide may form within N-acetylgalactosamine kinase between cysteines 301 and 303. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
2a2d
Structure name
x-ray structure of human n-acetyl galactosamine kinase complexed with mn-amppnp and n-acetyl glactosamine
Structure deposition date
2005-06-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
10
% buried
26
Peptide accession
Q01415
Residue number A
301
Residue number B
303
Peptide name
N-acetylgalactosamine kinase
Ligandability
Cysteine 301 of N-acetylgalactosamine kinase
Cysteine 303 of N-acetylgalactosamine kinase
2a2d A 229 A 407
A redox-regulated disulphide may form within N-acetylgalactosamine kinase between cysteines 229 and 407. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
2a2d
Structure name
x-ray structure of human n-acetyl galactosamine kinase complexed with mn-amppnp and n-acetyl glactosamine
Structure deposition date
2005-06-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
10
% buried
63
Peptide accession
Q01415
Residue number A
229
Residue number B
407
Peptide name
N-acetylgalactosamine kinase
Ligandability
Cysteine 229 of N-acetylgalactosamine kinase
Cysteine 407 of N-acetylgalactosamine kinase
2a2c A 113 A 175
A redox-regulated disulphide may form within N-acetylgalactosamine kinase between cysteines 113 and 175. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
2a2c
Structure name
x-ray structure of human n-acetyl galactosamine kinase complexed with mg-adp and n-acetyl galactosamine 1-phosphate
Structure deposition date
2005-06-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
91
Minimum pKa ?
9
% buried
96
Peptide accession
Q01415
Residue number A
113
Residue number B
175
Peptide name
N-acetylgalactosamine kinase
Ligandability
Cysteine 113 of N-acetylgalactosamine kinase
Cysteine 175 of N-acetylgalactosamine kinase
2a2d A 153 A 175
A redox-regulated disulphide may form within N-acetylgalactosamine kinase between cysteines 153 and 175. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
2a2d
Structure name
x-ray structure of human n-acetyl galactosamine kinase complexed with mn-amppnp and n-acetyl glactosamine
Structure deposition date
2005-06-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
103
Minimum pKa ?
9
% buried
100
Peptide accession
Q01415
Residue number A
153
Residue number B
175
Peptide name
N-acetylgalactosamine kinase
Ligandability
Cysteine 153 of N-acetylgalactosamine kinase
Cysteine 175 of N-acetylgalactosamine kinase
2a2d A 377 A 379
A redox-regulated disulphide may form within N-acetylgalactosamine kinase between cysteines 377 and 379. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
2a2d
Structure name
x-ray structure of human n-acetyl galactosamine kinase complexed with mn-amppnp and n-acetyl glactosamine
Structure deposition date
2005-06-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
76
Peptide accession
Q01415
Residue number A
377
Residue number B
379
Peptide name
N-acetylgalactosamine kinase
Ligandability
Cysteine 377 of N-acetylgalactosamine kinase
Cysteine 379 of N-acetylgalactosamine kinase
2a2c A 132 A 153
A redox-regulated disulphide may form within N-acetylgalactosamine kinase between cysteines 132 and 153. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
28
PDB code
2a2c
Structure name
x-ray structure of human n-acetyl galactosamine kinase complexed with mg-adp and n-acetyl galactosamine 1-phosphate
Structure deposition date
2005-06-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
99
Minimum pKa ?
13
% buried
100
Peptide accession
Q01415
Residue number A
132
Residue number B
153
Peptide name
N-acetylgalactosamine kinase
Ligandability
Cysteine 132 of N-acetylgalactosamine kinase
Cysteine 153 of N-acetylgalactosamine kinase
2a2c A 152 A 153
A redox-regulated disulphide may form within N-acetylgalactosamine kinase between cysteines 152 and 153. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
24
PDB code
2a2c
Structure name
x-ray structure of human n-acetyl galactosamine kinase complexed with mg-adp and n-acetyl galactosamine 1-phosphate
Structure deposition date
2005-06-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
109
Minimum pKa ?
13
% buried
100
Peptide accession
Q01415
Residue number A
152
Residue number B
153
Peptide name
N-acetylgalactosamine kinase
Ligandability
Cysteine 152 of N-acetylgalactosamine kinase
Cysteine 153 of N-acetylgalactosamine kinase
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