MBL associated serine protease 2
Intramolecular
Cysteine 152 and cysteine 165
Cysteine 241 and cysteine 259
Cysteine 142 and cysteine 156
Cysteine 72 and cysteine 90
Cysteine 167 and cysteine 180
Cysteine 184 and cysteine 211
Cysteine 152 and cysteine 156
Cysteine 156 and cysteine 165
Cysteine 142 and cysteine 152
Cysteine 142 and cysteine 165
More...Cysteine 165 and cysteine 180
Cysteine 165 and cysteine 167
Cysteine 152 and cysteine 180
Cysteine 152 and cysteine 167
5ckm A 133 A 146
A redox-regulated disulphide may form within MBL associated serine protease 2 between cysteines 152 and 165 (133 and 146 respectively in this structure).
Details
Redox score ?
89
PDB code
5ckm
Structure name
the cub1-egf-cub2 domains of rat mbl-associated serine protease-2 (masp-2) bound to ca2+
Structure deposition date
2015-07-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2VCV7
Residue number A
152
Residue number B
165
Peptide name
MBL associated serine protease 2
Ligandability
Cysteine 152 of MBL associated serine protease 2
Cysteine 165 of MBL associated serine protease 2
5cis A 222 A 240
A redox-regulated disulphide may form within MBL associated serine protease 2 between cysteines 241 and 259 (222 and 240 respectively in this structure).
Details
Redox score ?
88
PDB code
5cis
Structure name
the cub1-egf-cub2 domains of rat mbl-associated serine protease-2 (masp-2) bound to ca2+
Structure deposition date
2015-07-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2VCV7
Residue number A
241
Residue number B
259
Peptide name
MBL associated serine protease 2
Ligandability
Cysteine 241 of MBL associated serine protease 2
Cysteine 259 of MBL associated serine protease 2
5ckm A 123 A 137
A redox-regulated disulphide may form within MBL associated serine protease 2 between cysteines 142 and 156 (123 and 137 respectively in this structure).
Details
Redox score ?
86
PDB code
5ckm
Structure name
the cub1-egf-cub2 domains of rat mbl-associated serine protease-2 (masp-2) bound to ca2+
Structure deposition date
2015-07-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2VCV7
Residue number A
142
Residue number B
156
Peptide name
MBL associated serine protease 2
Ligandability
Cysteine 142 of MBL associated serine protease 2
Cysteine 156 of MBL associated serine protease 2
5ckn D 53 D 71
A redox-regulated disulphide may form within MBL associated serine protease 2 between cysteines 72 and 90 (53 and 71 respectively in this structure).
Details
Redox score ?
85
PDB code
5ckn
Structure name
the cub1-egf-cub2 domains of rat mbl-associated serine protease-2 (masp-2) bound to ca2+
Structure deposition date
2015-07-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2VCV7
Residue number A
72
Residue number B
90
Peptide name
MBL associated serine protease 2
Ligandability
Cysteine 72 of MBL associated serine protease 2
Cysteine 90 of MBL associated serine protease 2
5ckm A 148 A 161
A redox-regulated disulphide may form within MBL associated serine protease 2 between cysteines 167 and 180 (148 and 161 respectively in this structure).
Details
Redox score ?
84
PDB code
5ckm
Structure name
the cub1-egf-cub2 domains of rat mbl-associated serine protease-2 (masp-2) bound to ca2+
Structure deposition date
2015-07-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2VCV7
Residue number A
167
Residue number B
180
Peptide name
MBL associated serine protease 2
Ligandability
Cysteine 167 of MBL associated serine protease 2
Cysteine 180 of MBL associated serine protease 2
5cis A 165 A 192
A redox-regulated disulphide may form within MBL associated serine protease 2 between cysteines 184 and 211 (165 and 192 respectively in this structure).
Details
Redox score ?
84
PDB code
5cis
Structure name
the cub1-egf-cub2 domains of rat mbl-associated serine protease-2 (masp-2) bound to ca2+
Structure deposition date
2015-07-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2VCV7
Residue number A
184
Residue number B
211
Peptide name
MBL associated serine protease 2
Ligandability
Cysteine 184 of MBL associated serine protease 2
Cysteine 211 of MBL associated serine protease 2
5cis A 133 A 137
A redox-regulated disulphide may form within MBL associated serine protease 2 between cysteines 152 and 156 (133 and 137 respectively in this structure).
Details
Redox score ?
77
PDB code
5cis
Structure name
the cub1-egf-cub2 domains of rat mbl-associated serine protease-2 (masp-2) bound to ca2+
Structure deposition date
2015-07-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2VCV7
Residue number A
152
Residue number B
156
Peptide name
MBL associated serine protease 2
Ligandability
Cysteine 152 of MBL associated serine protease 2
Cysteine 156 of MBL associated serine protease 2
5ckm A 137 A 146
A redox-regulated disulphide may form within MBL associated serine protease 2 between cysteines 156 and 165 (137 and 146 respectively in this structure).
Details
Redox score ?
76
PDB code
5ckm
Structure name
the cub1-egf-cub2 domains of rat mbl-associated serine protease-2 (masp-2) bound to ca2+
Structure deposition date
2015-07-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2VCV7
Residue number A
156
Residue number B
165
Peptide name
MBL associated serine protease 2
Ligandability
Cysteine 156 of MBL associated serine protease 2
Cysteine 165 of MBL associated serine protease 2
5cis A 123 A 133
A redox-regulated disulphide may form within MBL associated serine protease 2 between cysteines 142 and 152 (123 and 133 respectively in this structure).
Details
Redox score ?
66
PDB code
5cis
Structure name
the cub1-egf-cub2 domains of rat mbl-associated serine protease-2 (masp-2) bound to ca2+
Structure deposition date
2015-07-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2VCV7
Residue number A
142
Residue number B
152
Peptide name
MBL associated serine protease 2
Ligandability
Cysteine 142 of MBL associated serine protease 2
Cysteine 152 of MBL associated serine protease 2
5cis A 123 A 146
A redox-regulated disulphide may form within MBL associated serine protease 2 between cysteines 142 and 165 (123 and 146 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
5cis
Structure name
the cub1-egf-cub2 domains of rat mbl-associated serine protease-2 (masp-2) bound to ca2+
Structure deposition date
2015-07-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2VCV7
Residue number A
142
Residue number B
165
Peptide name
MBL associated serine protease 2
Ligandability
Cysteine 142 of MBL associated serine protease 2
Cysteine 165 of MBL associated serine protease 2
5ckn D 146 D 161
A redox-regulated disulphide may form within MBL associated serine protease 2 between cysteines 165 and 180 (146 and 161 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
5ckn
Structure name
the cub1-egf-cub2 domains of rat mbl-associated serine protease-2 (masp-2) bound to ca2+
Structure deposition date
2015-07-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2VCV7
Residue number A
165
Residue number B
180
Peptide name
MBL associated serine protease 2
Ligandability
Cysteine 165 of MBL associated serine protease 2
Cysteine 180 of MBL associated serine protease 2
5ckm A 146 A 148
A redox-regulated disulphide may form within MBL associated serine protease 2 between cysteines 165 and 167 (146 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 ?
52
PDB code
5ckm
Structure name
the cub1-egf-cub2 domains of rat mbl-associated serine protease-2 (masp-2) bound to ca2+
Structure deposition date
2015-07-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2VCV7
Residue number A
165
Residue number B
167
Peptide name
MBL associated serine protease 2
Ligandability
Cysteine 165 of MBL associated serine protease 2
Cysteine 167 of MBL associated serine protease 2
5ckn D 133 D 161
A redox-regulated disulphide may form within MBL associated serine protease 2 between cysteines 152 and 180 (133 and 161 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
5ckn
Structure name
the cub1-egf-cub2 domains of rat mbl-associated serine protease-2 (masp-2) bound to ca2+
Structure deposition date
2015-07-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2VCV7
Residue number A
152
Residue number B
180
Peptide name
MBL associated serine protease 2
Ligandability
Cysteine 152 of MBL associated serine protease 2
Cysteine 180 of MBL associated serine protease 2
5ckn D 133 D 148
A redox-regulated disulphide may form within MBL associated serine protease 2 between cysteines 152 and 167 (133 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 ?
52
PDB code
5ckn
Structure name
the cub1-egf-cub2 domains of rat mbl-associated serine protease-2 (masp-2) bound to ca2+
Structure deposition date
2015-07-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
A2VCV7
Residue number A
152
Residue number B
167
Peptide name
MBL associated serine protease 2
Ligandability
Cysteine 152 of MBL associated serine protease 2
Cysteine 167 of MBL associated serine protease 2
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