Procollagen C-endopeptidase enhancer 1
Intramolecular
Cysteine 90 and cysteine 112
Cysteine 213 and cysteine 236
Cysteine 318 and cysteine 386
Cysteine 322 and cysteine 389
Cysteine 159 and cysteine 186
Cysteine 333 and cysteine 437
Cysteine 37 and cysteine 63
Cysteine 318 and cysteine 322
Cysteine 322 and cysteine 386
Cysteine 318 and cysteine 389
Cysteine 386 and cysteine 389
6fzw D 65 D 87
A redox-regulated disulphide may form within Procollagen C-endopeptidase enhancer 1 between cysteines 90 and 112 (65 and 87 respectively in this structure).
Details
Redox score ?
88
PDB code
6fzw
Structure name
crystal structure of the metalloproteinase enhancer pcpe-1 bound to the procollagen c propeptide trimer (long)
Structure deposition date
2018-03-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15113
Residue number A
90
Residue number B
112
Peptide name
Procollagen C-endopeptidase enhancer 1
Ligandability
Cysteine 90 of Procollagen C-endopeptidase enhancer 1
Cysteine 112 of Procollagen C-endopeptidase enhancer 1
6fzv D 188 D 211
A redox-regulated disulphide may form within Procollagen C-endopeptidase enhancer 1 between cysteines 213 and 236 (188 and 211 respectively in this structure).
Details
Redox score ?
87
PDB code
6fzv
Structure name
crystal structure of the metalloproteinase enhancer pcpe-1 bound to the procollagen c propeptide trimer (short)
Structure deposition date
2018-03-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15113
Residue number A
213
Residue number B
236
Peptide name
Procollagen C-endopeptidase enhancer 1
Ligandability
Cysteine 213 of Procollagen C-endopeptidase enhancer 1
Cysteine 236 of Procollagen C-endopeptidase enhancer 1
1uap A 30 A 98
A redox-regulated disulphide may form within Procollagen C-endopeptidase enhancer 1 between cysteines 318 and 386 (30 and 98 respectively in this structure).
Details
Redox score ?
86
PDB code
1uap
Structure name
nmr structure of the ntr domain from human pcolce1
Structure deposition date
2003-03-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15113
Residue number A
318
Residue number B
386
Peptide name
Procollagen C-endopeptidase enhancer 1
Ligandability
Cysteine 318 of Procollagen C-endopeptidase enhancer 1
Cysteine 386 of Procollagen C-endopeptidase enhancer 1
1uap A 34 A 101
A redox-regulated disulphide may form within Procollagen C-endopeptidase enhancer 1 between cysteines 322 and 389 (34 and 101 respectively in this structure).
Details
Redox score ?
85
PDB code
1uap
Structure name
nmr structure of the ntr domain from human pcolce1
Structure deposition date
2003-03-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15113
Residue number A
322
Residue number B
389
Peptide name
Procollagen C-endopeptidase enhancer 1
Ligandability
Cysteine 322 of Procollagen C-endopeptidase enhancer 1
Cysteine 389 of Procollagen C-endopeptidase enhancer 1
6fzv D 134 D 161
A redox-regulated disulphide may form within Procollagen C-endopeptidase enhancer 1 between cysteines 159 and 186 (134 and 161 respectively in this structure).
Details
Redox score ?
84
PDB code
6fzv
Structure name
crystal structure of the metalloproteinase enhancer pcpe-1 bound to the procollagen c propeptide trimer (short)
Structure deposition date
2018-03-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15113
Residue number A
159
Residue number B
186
Peptide name
Procollagen C-endopeptidase enhancer 1
Ligandability
Cysteine 159 of Procollagen C-endopeptidase enhancer 1
Cysteine 186 of Procollagen C-endopeptidase enhancer 1
1uap A 45 A 149
A redox-regulated disulphide may form within Procollagen C-endopeptidase enhancer 1 between cysteines 333 and 437 (45 and 149 respectively in this structure).
Details
Redox score ?
84
PDB code
1uap
Structure name
nmr structure of the ntr domain from human pcolce1
Structure deposition date
2003-03-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15113
Residue number A
333
Residue number B
437
Peptide name
Procollagen C-endopeptidase enhancer 1
Ligandability
Cysteine 333 of Procollagen C-endopeptidase enhancer 1
Cysteine 437 of Procollagen C-endopeptidase enhancer 1
6fzw D 12 D 38
A redox-regulated disulphide may form within Procollagen C-endopeptidase enhancer 1 between cysteines 37 and 63 (12 and 38 respectively in this structure).
Details
Redox score ?
83
PDB code
6fzw
Structure name
crystal structure of the metalloproteinase enhancer pcpe-1 bound to the procollagen c propeptide trimer (long)
Structure deposition date
2018-03-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15113
Residue number A
37
Residue number B
63
Peptide name
Procollagen C-endopeptidase enhancer 1
Ligandability
Cysteine 37 of Procollagen C-endopeptidase enhancer 1
Cysteine 63 of Procollagen C-endopeptidase enhancer 1
1uap A 30 A 34
A redox-regulated disulphide may form within Procollagen C-endopeptidase enhancer 1 between cysteines 318 and 322 (30 and 34 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
1uap
Structure name
nmr structure of the ntr domain from human pcolce1
Structure deposition date
2003-03-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15113
Residue number A
318
Residue number B
322
Peptide name
Procollagen C-endopeptidase enhancer 1
Ligandability
Cysteine 318 of Procollagen C-endopeptidase enhancer 1
Cysteine 322 of Procollagen C-endopeptidase enhancer 1
1uap A 34 A 98
A redox-regulated disulphide may form within Procollagen C-endopeptidase enhancer 1 between cysteines 322 and 386 (34 and 98 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
1uap
Structure name
nmr structure of the ntr domain from human pcolce1
Structure deposition date
2003-03-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15113
Residue number A
322
Residue number B
386
Peptide name
Procollagen C-endopeptidase enhancer 1
Ligandability
Cysteine 322 of Procollagen C-endopeptidase enhancer 1
Cysteine 386 of Procollagen C-endopeptidase enhancer 1
1uap A 30 A 101
A redox-regulated disulphide may form within Procollagen C-endopeptidase enhancer 1 between cysteines 318 and 389 (30 and 101 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
1uap
Structure name
nmr structure of the ntr domain from human pcolce1
Structure deposition date
2003-03-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15113
Residue number A
318
Residue number B
389
Peptide name
Procollagen C-endopeptidase enhancer 1
Ligandability
Cysteine 318 of Procollagen C-endopeptidase enhancer 1
Cysteine 389 of Procollagen C-endopeptidase enhancer 1
1uap A 98 A 101
A redox-regulated disulphide may form within Procollagen C-endopeptidase enhancer 1 between cysteines 386 and 389 (98 and 101 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
1uap
Structure name
nmr structure of the ntr domain from human pcolce1
Structure deposition date
2003-03-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15113
Residue number A
386
Residue number B
389
Peptide name
Procollagen C-endopeptidase enhancer 1
Ligandability
Cysteine 386 of Procollagen C-endopeptidase enhancer 1
Cysteine 389 of Procollagen C-endopeptidase enhancer 1
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