Pro-cathepsin H
Intermolecular
Cysteine 327 and cysteine 102
Intramolecular
Cysteine 272 and cysteine 322
Cysteine 172 and cysteine 214
Cysteine 102 and cysteine 327
Cysteine 138 and cysteine 181
Cysteine 138 and cysteine 141
Cysteine 141 and cysteine 181
1nb3 C 205 S 80
A redox-regulated disulphide may form between two units of Pro-cathepsin H at cysteines 327 and 102 (205 and 80 respectively in this structure).
Details
Redox score ?
77
PDB code
1nb3
Structure name
crystal structure of stefin a in complex with cathepsin h: n-terminal residues of inhibitors can adapt to the active sites of endo-and exopeptidases
Structure deposition date
2002-12-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
96
Minimum pKa ?
nan
% buried
nan
Peptide A name
Pro-cathepsin H
Peptide B name
Pro-cathepsin H
Peptide A accession
O46427
Peptide B accession
O46427
Peptide A residue number
327
Peptide B residue number
102
Ligandability
Cysteine 327 of Pro-cathepsin H
Cysteine 102 of Pro-cathepsin H
1nb3 B 154 B 200
A redox-regulated disulphide may form within Pro-cathepsin H between cysteines 272 and 322 (154 and 200 respectively in this structure).
Details
Redox score ?
85
PDB code
1nb3
Structure name
crystal structure of stefin a in complex with cathepsin h: n-terminal residues of inhibitors can adapt to the active sites of endo-and exopeptidases
Structure deposition date
2002-12-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
O46427
Residue number A
272
Residue number B
322
Peptide name
Pro-cathepsin H
Ligandability
Cysteine 272 of Pro-cathepsin H
Cysteine 322 of Pro-cathepsin H
6czk A 150 A 192
A redox-regulated disulphide may form within Pro-cathepsin H between cysteines 172 and 214 (150 and 192 respectively in this structure).
Details
Redox score ?
83
PDB code
6czk
Structure name
crystal structure of wild-type human pro-cathepsin h
Structure deposition date
2018-04-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09668
Residue number A
172
Residue number B
214
Peptide name
Pro-cathepsin H
Ligandability
Cysteine 172 of Pro-cathepsin H
Cysteine 214 of Pro-cathepsin H
6czs A 102 A 327
A redox-regulated disulphide may form within Pro-cathepsin H between cysteines 102 and 327.
Details
Redox score ?
80
PDB code
6czs
Structure name
crystal structure of human pro-cathepsin h c26s mutant
Structure deposition date
2018-04-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
92
Minimum pKa ?
nan
% buried
nan
Peptide accession
P09668
Residue number A
102
Residue number B
327
Peptide name
Pro-cathepsin H
Ligandability
Cysteine 102 of Pro-cathepsin H
Cysteine 327 of Pro-cathepsin H
1nb5 A 22 A 63
A redox-regulated disulphide may form within Pro-cathepsin H between cysteines 138 and 181 (22 and 63 respectively in this structure).
Details
Redox score ?
78
PDB code
1nb5
Structure name
crystal structure of stefin a in complex with cathepsin h
Structure deposition date
2002-12-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
O46427
Residue number A
138
Residue number B
181
Peptide name
Pro-cathepsin H
Ligandability
Cysteine 138 of Pro-cathepsin H
Cysteine 181 of Pro-cathepsin H
1nb3 D 22 D 25
A redox-regulated disulphide may form within Pro-cathepsin H between cysteines 138 and 141 (22 and 25 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
1nb3
Structure name
crystal structure of stefin a in complex with cathepsin h: n-terminal residues of inhibitors can adapt to the active sites of endo-and exopeptidases
Structure deposition date
2002-12-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
94
Minimum pKa ?
12
% buried
nan
Peptide accession
O46427
Residue number A
138
Residue number B
141
Peptide name
Pro-cathepsin H
Ligandability
Cysteine 138 of Pro-cathepsin H
Cysteine 141 of Pro-cathepsin H
1nb3 A 25 A 63
A redox-regulated disulphide may form within Pro-cathepsin H between cysteines 141 and 181 (25 and 63 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
26
PDB code
1nb3
Structure name
crystal structure of stefin a in complex with cathepsin h: n-terminal residues of inhibitors can adapt to the active sites of endo-and exopeptidases
Structure deposition date
2002-12-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
98
Minimum pKa ?
11
% buried
nan
Peptide accession
O46427
Residue number A
141
Residue number B
181
Peptide name
Pro-cathepsin H
Ligandability
Cysteine 141 of Pro-cathepsin H
Cysteine 181 of Pro-cathepsin H
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