Chymotrypsin-C
Intermolecular
Cysteine 141 and cysteine 17
Intramolecular
Cysteine 155 and cysteine 222
Cysteine 186 and cysteine 202
Cysteine 59 and cysteine 75
Cysteine 212 and cysteine 243
4h4f A 122 Q 1
A redox-regulated disulphide may form between two units of Chymotrypsin-C at cysteines 141 and 17 (122 and 1 respectively in this structure).
Details
Redox score ?
85
PDB code
4h4f
Structure name
crystal structure of human chymotrypsin c (ctrc) bound to inhibitor eglin c from hirudo medicinalis
Structure deposition date
2012-09-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chymotrypsin-C
Peptide B name
Chymotrypsin-C
Peptide A accession
Q99895
Peptide B accession
Q99895
Peptide A residue number
141
Peptide B residue number
17
Ligandability
Cysteine 141 of Chymotrypsin-C
Cysteine 17 of Chymotrypsin-C
4h4f A 136 A 201
A redox-regulated disulphide may form within Chymotrypsin-C between cysteines 155 and 222 (136 and 201 respectively in this structure).
Details
Redox score ?
81
PDB code
4h4f
Structure name
crystal structure of human chymotrypsin c (ctrc) bound to inhibitor eglin c from hirudo medicinalis
Structure deposition date
2012-09-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99895
Residue number A
155
Residue number B
222
Peptide name
Chymotrypsin-C
Ligandability
Cysteine 155 of Chymotrypsin-C
Cysteine 222 of Chymotrypsin-C
4h4f A 168 A 182
A redox-regulated disulphide may form within Chymotrypsin-C between cysteines 186 and 202 (168 and 182 respectively in this structure).
Details
Redox score ?
80
PDB code
4h4f
Structure name
crystal structure of human chymotrypsin c (ctrc) bound to inhibitor eglin c from hirudo medicinalis
Structure deposition date
2012-09-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99895
Residue number A
186
Residue number B
202
Peptide name
Chymotrypsin-C
Ligandability
Cysteine 186 of Chymotrypsin-C
Cysteine 202 of Chymotrypsin-C
4h4f A 42 A 58
A redox-regulated disulphide may form within Chymotrypsin-C between cysteines 59 and 75 (42 and 58 respectively in this structure).
Details
Redox score ?
80
PDB code
4h4f
Structure name
crystal structure of human chymotrypsin c (ctrc) bound to inhibitor eglin c from hirudo medicinalis
Structure deposition date
2012-09-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
93
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99895
Residue number A
59
Residue number B
75
Peptide name
Chymotrypsin-C
Ligandability
Cysteine 59 of Chymotrypsin-C
Cysteine 75 of Chymotrypsin-C
4h4f A 191 A 220
A redox-regulated disulphide may form within Chymotrypsin-C between cysteines 212 and 243 (191 and 220 respectively in this structure).
Details
Redox score ?
77
PDB code
4h4f
Structure name
crystal structure of human chymotrypsin c (ctrc) bound to inhibitor eglin c from hirudo medicinalis
Structure deposition date
2012-09-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
98
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q99895
Residue number A
212
Residue number B
243
Peptide name
Chymotrypsin-C
Ligandability
Cysteine 212 of Chymotrypsin-C
Cysteine 243 of Chymotrypsin-C
If this tool was useful for finding a disulphide, please cite: