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Refinement of the structure of human basic fibroblast growth factor at 1.6 ångströms resolution and analysis of presumed heparin binding sites by selenate substitution

Analyse Refinement of the structure of human basic fibroblast growth factor at 1.6… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1FGA
Type: protein
Length: 124 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Basic fibroblast growth factor
UniProt: P09038
Ligands: SE4

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Basic fibroblast growth factor	protein	124	7% helix, 37% strand	P09038

Ligands and binding sites

SE4 · Selenate ion · ion · 2 copies · chains A
BME · Beta-mercaptoethanol · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Modifications

Observed in the structure: 2 covalent (additive adduct).

Compared structures

1FGA · Refinement of the structure of human basic fibroblast growth factor at 1.6 ångströms… · the same entry in another collection · chain A against A, TM-score 1.00
P09038 · AlphaFold monomer V2.0 prediction for fibroblast growth factor 2 (P09038) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P09038
Elsewhere: RCSB PDB 1FGA · PDBe 1FGA · UniProt P09038

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