ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Fibroblast growth factor 2

Intermolecular
Cysteine 211 and cysteine 211
Intramolecular
Cysteine 229 and cysteine 234
A redox-regulated disulphide may form between two units of Fibroblast growth factor 2 at cysteines 211 and 211 (69 and 69 respectively in this structure).

Details

Redox score ?
80
PDB code
5x1o
Structure name
pi(4,5)p2 lipid binding induced a reorientation of fgf2 molecules near membrane surface to facilitate the unconventional oligomerization- dependent secretion process as revealed by a combined ftir/nmr/x-ray study
Structure deposition date
2017-01-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide A name
Fibroblast growth factor 2
Peptide B name
Fibroblast growth factor 2
Peptide A accession
P09038
Peptide B accession
P09038
Peptide A residue number
211
Peptide B residue number
211

Ligandability

A redox-regulated disulphide may form within Fibroblast growth factor 2 between cysteines 229 and 234 (87 and 92 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
5x1o
Structure name
pi(4,5)p2 lipid binding induced a reorientation of fgf2 molecules near membrane surface to facilitate the unconventional oligomerization- dependent secretion process as revealed by a combined ftir/nmr/x-ray study
Structure deposition date
2017-01-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
28
Peptide accession
P09038
Residue number A
229
Residue number B
234
Peptide name
Fibroblast growth factor 2

Ligandability

Cysteine 229 of Fibroblast growth factor 2

Cysteine 234 of Fibroblast growth factor 2

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