Betaine--homocysteine S-methyltransferase 1
Intramolecular
Cysteine 217 and cysteine 299
Cysteine 217 and cysteine 300
Cysteine 299 and cysteine 300
Cysteine 186 and cysteine 217
Cysteine 186 and cysteine 299
Cysteine 186 and cysteine 256
Cysteine 217 and cysteine 256
Cysteine 186 and cysteine 300
1lt8 B 217 B 299
A redox-regulated disulphide may form within Betaine--homocysteine S-methyltransferase 1 between cysteines 217 and 299.
Details
Redox score ?
60
PDB code
1lt8
Structure name
reduced homo sapiens betaine-homocysteine s-methyltransferase in complex with s-(delta-carboxybutyl)-l-homocysteine
Structure deposition date
2002-05-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
nan
Peptide accession
Q93088
Residue number A
217
Residue number B
299
Peptide name
Betaine--homocysteine S-methyltransferase 1
Ligandability
Cysteine 217 of Betaine--homocysteine S-methyltransferase 1
Cysteine 299 of Betaine--homocysteine S-methyltransferase 1
4m3p A 217 A 300
A redox-regulated disulphide may form within Betaine--homocysteine S-methyltransferase 1 between cysteines 217 and 300. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
4m3p
Structure name
betaine-homocysteine s-methyltransferase from homo sapiens complexed with homocysteine
Structure deposition date
2013-08-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
83
Minimum pKa ?
14
% buried
100
Peptide accession
Q93088
Residue number A
217
Residue number B
300
Peptide name
Betaine--homocysteine S-methyltransferase 1
Ligandability
Cysteine 217 of Betaine--homocysteine S-methyltransferase 1
Cysteine 300 of Betaine--homocysteine S-methyltransferase 1
1lt8 B 299 B 300
A redox-regulated disulphide may form within Betaine--homocysteine S-methyltransferase 1 between cysteines 299 and 300. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
1lt8
Structure name
reduced homo sapiens betaine-homocysteine s-methyltransferase in complex with s-(delta-carboxybutyl)-l-homocysteine
Structure deposition date
2002-05-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
84
Minimum pKa ?
22
% buried
nan
Peptide accession
Q93088
Residue number A
299
Residue number B
300
Peptide name
Betaine--homocysteine S-methyltransferase 1
Ligandability
Cysteine 299 of Betaine--homocysteine S-methyltransferase 1
Cysteine 300 of Betaine--homocysteine S-methyltransferase 1
4m3p C 186 C 217
A redox-regulated disulphide may form within Betaine--homocysteine S-methyltransferase 1 between cysteines 186 and 217. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
4m3p
Structure name
betaine-homocysteine s-methyltransferase from homo sapiens complexed with homocysteine
Structure deposition date
2013-08-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
88
Minimum pKa ?
14
% buried
100
Peptide accession
Q93088
Residue number A
186
Residue number B
217
Peptide name
Betaine--homocysteine S-methyltransferase 1
Ligandability
Cysteine 186 of Betaine--homocysteine S-methyltransferase 1
Cysteine 217 of Betaine--homocysteine S-methyltransferase 1
4m3p C 186 C 299
A redox-regulated disulphide may form within Betaine--homocysteine S-methyltransferase 1 between cysteines 186 and 299. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
4m3p
Structure name
betaine-homocysteine s-methyltransferase from homo sapiens complexed with homocysteine
Structure deposition date
2013-08-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
14
% buried
nan
Peptide accession
Q93088
Residue number A
186
Residue number B
299
Peptide name
Betaine--homocysteine S-methyltransferase 1
Ligandability
Cysteine 186 of Betaine--homocysteine S-methyltransferase 1
Cysteine 299 of Betaine--homocysteine S-methyltransferase 1
1umy D 186 D 256
A redox-regulated disulphide may form within Betaine--homocysteine S-methyltransferase 1 between cysteines 186 and 256. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
27
PDB code
1umy
Structure name
bhmt from rat liver
Structure deposition date
2003-09-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
96
Peptide accession
O09171
Residue number A
186
Residue number B
256
Peptide name
Betaine--homocysteine S-methyltransferase 1
Ligandability
Cysteine 186 of Betaine--homocysteine S-methyltransferase 1
Cysteine 256 of Betaine--homocysteine S-methyltransferase 1
4m3p A 217 A 256
A redox-regulated disulphide may form within Betaine--homocysteine S-methyltransferase 1 between cysteines 217 and 256. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
24
PDB code
4m3p
Structure name
betaine-homocysteine s-methyltransferase from homo sapiens complexed with homocysteine
Structure deposition date
2013-08-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
13
% buried
98
Peptide accession
Q93088
Residue number A
217
Residue number B
256
Peptide name
Betaine--homocysteine S-methyltransferase 1
Ligandability
Cysteine 217 of Betaine--homocysteine S-methyltransferase 1
Cysteine 256 of Betaine--homocysteine S-methyltransferase 1
4m3p A 186 A 300
A redox-regulated disulphide may form within Betaine--homocysteine S-methyltransferase 1 between cysteines 186 and 300. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
18
PDB code
4m3p
Structure name
betaine-homocysteine s-methyltransferase from homo sapiens complexed with homocysteine
Structure deposition date
2013-08-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
14
% buried
100
Peptide accession
Q93088
Residue number A
186
Residue number B
300
Peptide name
Betaine--homocysteine S-methyltransferase 1
Ligandability
Cysteine 186 of Betaine--homocysteine S-methyltransferase 1
Cysteine 300 of Betaine--homocysteine S-methyltransferase 1
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