ADP-ribosylation factor 1
3o47 A 289 B 289
A redox-regulated disulphide may form between two units of ADP-ribosylation factor 1 at cysteines 159 and 159 (289 and 289 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
3o47
Structure name
crystal structure of arfgap1-arf1 fusion protein
Structure deposition date
2010-07-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
9
% buried
54
Peptide A name
ADP-ribosylation factor 1
Peptide B name
ADP-ribosylation factor 1
Peptide A accession
P84077
Peptide B accession
P84077
Peptide A residue number
159
Peptide B residue number
159
Ligandability
3o47 B 22 B 42
A redox-regulated disulphide may form within ADP-ribosylation factor 1 between cysteines 22 and 42.
Details
Redox score ?
nan
PDB code
3o47
Structure name
crystal structure of arfgap1-arf1 fusion protein
Structure deposition date
2010-07-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
3
% buried
44
Peptide accession
P84077
Residue number A
22
Residue number B
42
Peptide name
ADP-ribosylation factor 1
Ligandability
Cysteine 22 of ADP-ribosylation factor 1
Cysteine 42 of ADP-ribosylation factor 1
Cysteine 22 in protein A could not be asigned to a Uniprot residue.
Cysteine 42 in protein B could not be asigned to a Uniprot residue.
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