Pro-epidermal growth factor
Intramolecular
Cysteine 976 and cysteine 990
Cysteine 1003 and cysteine 1012
Cysteine 984 and cysteine 1001
Cysteine 976 and cysteine 984
Cysteine 976 and cysteine 1001
Cysteine 984 and cysteine 990
Cysteine 1001 and cysteine 1012
Cysteine 984 and cysteine 1012
Cysteine 1001 and cysteine 1003
Cysteine 990 and cysteine 1001
More...Cysteine 984 and cysteine 1003
Cysteine 976 and cysteine 1003
Cysteine 976 and cysteine 1012
Cysteine 990 and cysteine 1003
Cysteine 990 and cysteine 1012
7om4 C 6 C 20
A redox-regulated disulphide may form within Pro-epidermal growth factor between cysteines 976 and 990 (6 and 20 respectively in this structure).
Details
Redox score ?
88
PDB code
7om4
Structure name
nanobody egb4 bound to the full extracellular egfr-egf complex
Structure deposition date
2021-05-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01133
Residue number A
976
Residue number B
990
Peptide name
Pro-epidermal growth factor
Ligandability
Cysteine 976 of Pro-epidermal growth factor
Cysteine 990 of Pro-epidermal growth factor
1jl9 B 33 B 42
A redox-regulated disulphide may form within Pro-epidermal growth factor between cysteines 1003 and 1012 (33 and 42 respectively in this structure).
Details
Redox score ?
87
PDB code
1jl9
Structure name
crystal structure of human epidermal growth factor
Structure deposition date
2001-07-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01133
Residue number A
1003
Residue number B
1012
Peptide name
Pro-epidermal growth factor
Ligandability
Cysteine 1003 of Pro-epidermal growth factor
Cysteine 1012 of Pro-epidermal growth factor
1nql B 14 B 31
A redox-regulated disulphide may form within Pro-epidermal growth factor between cysteines 984 and 1001 (14 and 31 respectively in this structure).
Details
Redox score ?
85
PDB code
1nql
Structure name
structure of the extracellular domain of human epidermal growth factor (egf) receptor in an inactive (low ph) complex with egf
Structure deposition date
2003-01-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01133
Residue number A
984
Residue number B
1001
Peptide name
Pro-epidermal growth factor
Ligandability
Cysteine 984 of Pro-epidermal growth factor
Cysteine 1001 of Pro-epidermal growth factor
1nql B 6 B 14
A redox-regulated disulphide may form within Pro-epidermal growth factor between cysteines 976 and 984 (6 and 14 respectively in this structure).
Details
Redox score ?
76
PDB code
1nql
Structure name
structure of the extracellular domain of human epidermal growth factor (egf) receptor in an inactive (low ph) complex with egf
Structure deposition date
2003-01-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01133
Residue number A
976
Residue number B
984
Peptide name
Pro-epidermal growth factor
Ligandability
Cysteine 976 of Pro-epidermal growth factor
Cysteine 984 of Pro-epidermal growth factor
1nql B 6 B 31
A redox-regulated disulphide may form within Pro-epidermal growth factor between cysteines 976 and 1001 (6 and 31 respectively in this structure).
Details
Redox score ?
73
PDB code
1nql
Structure name
structure of the extracellular domain of human epidermal growth factor (egf) receptor in an inactive (low ph) complex with egf
Structure deposition date
2003-01-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01133
Residue number A
976
Residue number B
1001
Peptide name
Pro-epidermal growth factor
Ligandability
Cysteine 976 of Pro-epidermal growth factor
Cysteine 1001 of Pro-epidermal growth factor
1ivo D 14 D 20
A redox-regulated disulphide may form within Pro-epidermal growth factor between cysteines 984 and 990 (14 and 20 respectively in this structure).
Details
Redox score ?
71
PDB code
1ivo
Structure name
crystal structure of the complex of human epidermal growth factor and receptor extracellular domains
Structure deposition date
2002-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01133
Residue number A
984
Residue number B
990
Peptide name
Pro-epidermal growth factor
Ligandability
Cysteine 984 of Pro-epidermal growth factor
Cysteine 990 of Pro-epidermal growth factor
1ivo C 31 C 42
A redox-regulated disulphide may form within Pro-epidermal growth factor between cysteines 1001 and 1012 (31 and 42 respectively in this structure).
Details
Redox score ?
69
PDB code
1ivo
Structure name
crystal structure of the complex of human epidermal growth factor and receptor extracellular domains
Structure deposition date
2002-03-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01133
Residue number A
1001
Residue number B
1012
Peptide name
Pro-epidermal growth factor
Ligandability
Cysteine 1001 of Pro-epidermal growth factor
Cysteine 1012 of Pro-epidermal growth factor
1jl9 A 14 A 42
A redox-regulated disulphide may form within Pro-epidermal growth factor between cysteines 984 and 1012 (14 and 42 respectively in this structure).
Details
Redox score ?
68
PDB code
1jl9
Structure name
crystal structure of human epidermal growth factor
Structure deposition date
2001-07-16
Thiol separation (Å)
5
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01133
Residue number A
984
Residue number B
1012
Peptide name
Pro-epidermal growth factor
Ligandability
Cysteine 984 of Pro-epidermal growth factor
Cysteine 1012 of Pro-epidermal growth factor
1ivo D 31 D 33
A redox-regulated disulphide may form within Pro-epidermal growth factor between cysteines 1001 and 1003 (31 and 33 respectively in this structure).
Details
Redox score ?
66
PDB code
1ivo
Structure name
crystal structure of the complex of human epidermal growth factor and receptor extracellular domains
Structure deposition date
2002-03-28
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01133
Residue number A
1001
Residue number B
1003
Peptide name
Pro-epidermal growth factor
Ligandability
Cysteine 1001 of Pro-epidermal growth factor
Cysteine 1003 of Pro-epidermal growth factor
1jl9 A 20 A 31
A redox-regulated disulphide may form within Pro-epidermal growth factor between cysteines 990 and 1001 (20 and 31 respectively in this structure).
Details
Redox score ?
65
PDB code
1jl9
Structure name
crystal structure of human epidermal growth factor
Structure deposition date
2001-07-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01133
Residue number A
990
Residue number B
1001
Peptide name
Pro-epidermal growth factor
Ligandability
Cysteine 990 of Pro-epidermal growth factor
Cysteine 1001 of Pro-epidermal growth factor
1jl9 B 14 B 33
A redox-regulated disulphide may form within Pro-epidermal growth factor between cysteines 984 and 1003 (14 and 33 respectively in this structure).
Details
Redox score ?
64
PDB code
1jl9
Structure name
crystal structure of human epidermal growth factor
Structure deposition date
2001-07-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01133
Residue number A
984
Residue number B
1003
Peptide name
Pro-epidermal growth factor
Ligandability
Cysteine 984 of Pro-epidermal growth factor
Cysteine 1003 of Pro-epidermal growth factor
1jl9 B 6 B 33
A redox-regulated disulphide may form within Pro-epidermal growth factor between cysteines 976 and 1003 (6 and 33 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
1jl9
Structure name
crystal structure of human epidermal growth factor
Structure deposition date
2001-07-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01133
Residue number A
976
Residue number B
1003
Peptide name
Pro-epidermal growth factor
Ligandability
Cysteine 976 of Pro-epidermal growth factor
Cysteine 1003 of Pro-epidermal growth factor
1nql B 6 B 42
A redox-regulated disulphide may form within Pro-epidermal growth factor between cysteines 976 and 1012 (6 and 42 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
1nql
Structure name
structure of the extracellular domain of human epidermal growth factor (egf) receptor in an inactive (low ph) complex with egf
Structure deposition date
2003-01-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01133
Residue number A
976
Residue number B
1012
Peptide name
Pro-epidermal growth factor
Ligandability
Cysteine 976 of Pro-epidermal growth factor
Cysteine 1012 of Pro-epidermal growth factor
1p9j A 22 A 35
A redox-regulated disulphide may form within Pro-epidermal growth factor between cysteines 990 and 1003 (22 and 35 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
1p9j
Structure name
solution structure and dynamics of the egf/tgf-alpha chimera t1e
Structure deposition date
2003-05-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01133
Residue number A
990
Residue number B
1003
Peptide name
Pro-epidermal growth factor
Ligandability
Cysteine 990 of Pro-epidermal growth factor
Cysteine 1003 of Pro-epidermal growth factor
1ivo C 20 C 42
A redox-regulated disulphide may form within Pro-epidermal growth factor between cysteines 990 and 1012 (20 and 42 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
1ivo
Structure name
crystal structure of the complex of human epidermal growth factor and receptor extracellular domains
Structure deposition date
2002-03-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01133
Residue number A
990
Residue number B
1012
Peptide name
Pro-epidermal growth factor
Ligandability
Cysteine 990 of Pro-epidermal growth factor
Cysteine 1012 of Pro-epidermal growth factor
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