Sphingosine-1-phosphate lyase 1
Intermolecular
Cysteine 475 of Mannan-binding lectin serine protease 1 and cysteine 70
Cysteine 491 of Mannan-binding lectin serine protease 1 and cysteine 70
Cysteine 672 of Mannan-binding lectin serine protease 1 and cysteine 84
Cysteine 475 of Mannan-binding lectin serine protease 1 and cysteine 89
Intramolecular
Cysteine 193 and cysteine 203
Cysteine 203 and cysteine 205
Cysteine 193 and cysteine 205
4djz D 475 I 17
A redox-regulated disulphide may form between cysteine 475 of Mannan-binding lectin serine protease 1 and cysteine 70 of Serine protease inhibitor I/II (475 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 ?
43
PDB code
4djz
Structure name
catalytic fragment of masp-1 in complex with its specific inhibitor developed by directed evolution on sgci scaffold
Structure deposition date
2012-02-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide A name
Mannan-binding lectin serine protease 1
Peptide B name
Serine protease inhibitor I/II
Peptide A accession
P48740
Peptide B accession
O46162
Peptide A residue number
475
Peptide B residue number
70
Ligandability
Cysteine 475 of Mannan-binding lectin serine protease 1
Cysteine 70 of Serine protease inhibitor I/II
4djz D 491 I 17
A redox-regulated disulphide may form between cysteine 491 of Mannan-binding lectin serine protease 1 and cysteine 70 of Serine protease inhibitor I/II (491 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 ?
39
PDB code
4djz
Structure name
catalytic fragment of masp-1 in complex with its specific inhibitor developed by directed evolution on sgci scaffold
Structure deposition date
2012-02-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide A name
Mannan-binding lectin serine protease 1
Peptide B name
Serine protease inhibitor I/II
Peptide A accession
P48740
Peptide B accession
O46162
Peptide A residue number
491
Peptide B residue number
70
Ligandability
Cysteine 491 of Mannan-binding lectin serine protease 1
Cysteine 70 of Serine protease inhibitor I/II
4djz B 672 H 31
A redox-regulated disulphide may form between cysteine 672 of Mannan-binding lectin serine protease 1 and cysteine 84 of Serine protease inhibitor I/II (672 and 31 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
4djz
Structure name
catalytic fragment of masp-1 in complex with its specific inhibitor developed by directed evolution on sgci scaffold
Structure deposition date
2012-02-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide A name
Mannan-binding lectin serine protease 1
Peptide B name
Serine protease inhibitor I/II
Peptide A accession
P48740
Peptide B accession
O46162
Peptide A residue number
672
Peptide B residue number
84
Ligandability
Cysteine 672 of Mannan-binding lectin serine protease 1
Cysteine 84 of Serine protease inhibitor I/II
4djz D 475 I 36
A redox-regulated disulphide may form between cysteine 475 of Mannan-binding lectin serine protease 1 and cysteine 89 of Serine protease inhibitor I/II (475 and 36 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
4djz
Structure name
catalytic fragment of masp-1 in complex with its specific inhibitor developed by directed evolution on sgci scaffold
Structure deposition date
2012-02-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide A name
Mannan-binding lectin serine protease 1
Peptide B name
Serine protease inhibitor I/II
Peptide A accession
P48740
Peptide B accession
O46162
Peptide A residue number
475
Peptide B residue number
89
Ligandability
Cysteine 475 of Mannan-binding lectin serine protease 1
Cysteine 89 of Serine protease inhibitor I/II
4q6r B 193 B 203
A redox-regulated disulphide may form within Sphingosine-1-phosphate lyase 1 between cysteines 193 and 203. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
4q6r
Structure name
crystal structure of human sphingosine-1-phosphate lyase in complex with inhibitor 6-[(2r)-4-(4-benzyl-7-chlorophthalazin-1-yl)-2- methylpiperazin-1-yl]pyridine-3-carbonitrile
Structure deposition date
2014-04-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
83
Minimum pKa ?
10
% buried
94
Peptide accession
O95470
Residue number A
193
Residue number B
203
Peptide name
Sphingosine-1-phosphate lyase 1
Ligandability
Cysteine 193 of Sphingosine-1-phosphate lyase 1
Cysteine 203 of Sphingosine-1-phosphate lyase 1
4q6r A 203 A 205
A redox-regulated disulphide may form within Sphingosine-1-phosphate lyase 1 between cysteines 203 and 205. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
4q6r
Structure name
crystal structure of human sphingosine-1-phosphate lyase in complex with inhibitor 6-[(2r)-4-(4-benzyl-7-chlorophthalazin-1-yl)-2- methylpiperazin-1-yl]pyridine-3-carbonitrile
Structure deposition date
2014-04-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
95
Minimum pKa ?
11
% buried
94
Peptide accession
O95470
Residue number A
203
Residue number B
205
Peptide name
Sphingosine-1-phosphate lyase 1
Ligandability
Cysteine 203 of Sphingosine-1-phosphate lyase 1
Cysteine 205 of Sphingosine-1-phosphate lyase 1
4q6r A 193 A 205
A redox-regulated disulphide may form within Sphingosine-1-phosphate lyase 1 between cysteines 193 and 205. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
27
PDB code
4q6r
Structure name
crystal structure of human sphingosine-1-phosphate lyase in complex with inhibitor 6-[(2r)-4-(4-benzyl-7-chlorophthalazin-1-yl)-2- methylpiperazin-1-yl]pyridine-3-carbonitrile
Structure deposition date
2014-04-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
91
Minimum pKa ?
10
% buried
100
Peptide accession
O95470
Residue number A
193
Residue number B
205
Peptide name
Sphingosine-1-phosphate lyase 1
Ligandability
Cysteine 193 of Sphingosine-1-phosphate lyase 1
Cysteine 205 of Sphingosine-1-phosphate lyase 1
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