Cell division control protein 42 homolog
Intramolecular
Cysteine 105 and cysteine 188
Cysteine 18 and cysteine 81
Cysteine 6 and cysteine 105
Cysteine 81 and cysteine 157
Cysteine 6 and cysteine 81
Cysteine 6 and cysteine 18
Cysteine 18 and cysteine 157
Cysteine 6 and cysteine 157
Cysteine 212 and cysteine 285
1grn A 105 A 188
A redox-regulated disulphide may form within Cell division control protein 42 homolog between cysteines 105 and 188.
Details
Redox score ?
88
PDB code
1grn
Structure name
crystal structure of the cdc42/cdc42gap/alf3 complex
Structure deposition date
1998-07-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P60953
Residue number A
105
Residue number B
188
Peptide name
Cell division control protein 42 homolog
Ligandability
Cysteine 105 of Cell division control protein 42 homolog
Cysteine 188 of Cell division control protein 42 homolog
1e0a A 18 A 81
A redox-regulated disulphide may form within Cell division control protein 42 homolog between cysteines 18 and 81. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
1e0a
Structure name
cdc42 complexed with the gtpase binding domain of p21 activated kinase
Structure deposition date
2000-03-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
97
Peptide accession
P60953
Residue number A
18
Residue number B
81
Peptide name
Cell division control protein 42 homolog
Ligandability
Cysteine 18 of Cell division control protein 42 homolog
Cysteine 81 of Cell division control protein 42 homolog
1aje A 6 A 105
A redox-regulated disulphide may form within Cell division control protein 42 homolog between cysteines 6 and 105. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
1aje
Structure name
cdc42 from human, nmr, 20 structures
Structure deposition date
1997-05-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
60
Peptide accession
P60953
Residue number A
6
Residue number B
105
Peptide name
Cell division control protein 42 homolog
Ligandability
Cysteine 6 of Cell division control protein 42 homolog
Cysteine 105 of Cell division control protein 42 homolog
3eg5 C 81 C 157
A redox-regulated disulphide may form within Cell division control protein 42 homolog between cysteines 81 and 157. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
3eg5
Structure name
crystal structure of mdia1-tsh gbd-fh3 in complex with cdc42-gmppnp
Structure deposition date
2008-09-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
100
Peptide accession
P60766
Residue number A
81
Residue number B
157
Peptide name
Cell division control protein 42 homolog
Ligandability
Cysteine 81 of Cell division control protein 42 homolog
Cysteine 157 of Cell division control protein 42 homolog
3eg5 C 6 C 81
A redox-regulated disulphide may form within Cell division control protein 42 homolog between cysteines 6 and 81. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
3eg5
Structure name
crystal structure of mdia1-tsh gbd-fh3 in complex with cdc42-gmppnp
Structure deposition date
2008-09-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
95
Minimum pKa ?
12
% buried
100
Peptide accession
P60766
Residue number A
6
Residue number B
81
Peptide name
Cell division control protein 42 homolog
Ligandability
Cysteine 6 of Cell division control protein 42 homolog
Cysteine 81 of Cell division control protein 42 homolog
1ees A 6 A 18
A redox-regulated disulphide may form within Cell division control protein 42 homolog between cysteines 6 and 18. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
1ees
Structure name
solution structure of cdc42hs complexed with a peptide derived from p- 21 activated kinase, nmr, 20 structures
Structure deposition date
2000-02-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
93
Peptide accession
P60953
Residue number A
6
Residue number B
18
Peptide name
Cell division control protein 42 homolog
Ligandability
Cysteine 6 of Cell division control protein 42 homolog
Cysteine 18 of Cell division control protein 42 homolog
6tky D 18 D 157
A redox-regulated disulphide may form within Cell division control protein 42 homolog between cysteines 18 and 157. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
6tky
Structure name
crystal structure of the dhr2 domain of dock10 in complex with cdc42
Structure deposition date
2019-11-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
86
Peptide accession
P60953
Residue number A
18
Residue number B
157
Peptide name
Cell division control protein 42 homolog
Ligandability
Cysteine 18 of Cell division control protein 42 homolog
Cysteine 157 of Cell division control protein 42 homolog
1cee A 6 A 157
A redox-regulated disulphide may form within Cell division control protein 42 homolog between cysteines 6 and 157. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
25
PDB code
1cee
Structure name
solution structure of cdc42 in complex with the gtpase binding domain of wasp
Structure deposition date
1999-03-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
100
Peptide accession
P60953
Residue number A
6
Residue number B
157
Peptide name
Cell division control protein 42 homolog
Ligandability
Cysteine 6 of Cell division control protein 42 homolog
Cysteine 157 of Cell division control protein 42 homolog
6sup A 212 A 285
A redox-regulated disulphide may form within Cell division control protein 42 homolog between cysteines 212 and 285.
Details
Redox score ?
nan
PDB code
6sup
Structure name
crystal structure of tcdb2-tccc3-cdc42
Structure deposition date
2019-09-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P60953
Residue number A
212
Residue number B
285
Peptide name
Cell division control protein 42 homolog
Ligandability
Cysteine 212 of Cell division control protein 42 homolog
Cysteine 285 of Cell division control protein 42 homolog
Cysteine 212 in protein A could not be asigned to a Uniprot residue.
Cysteine 285 in protein B could not be asigned to a Uniprot residue.
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