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Crystal structure of FGF-1, S50E/V51N

Analyse Crystal structure of FGF-1, S50E/V51N in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Q04
Type: protein
Length: 282 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heparin-binding growth factor 1
UniProt: P05230
Pockets: 1 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Heparin-binding growth factor 1	protein	141	6% helix, 38% strand	P05230

Ligands and binding sites

FMT · Formic acid · additive · 4 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	121	0.40	0.75	23	empty

Interfaces

1 interface between chains.

A–B · 455 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

1Q04 · Crystal structure of FGF-1, S50E/V51N · the same entry in another collection · chain A against A, TM-score 1.00
P05230 · AlphaFold monomer V2.0 prediction for fibroblast growth factor 1 (P05230) · a predicted model of the same protein · chain B against A, TM-score 0.96

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 P05230
Elsewhere: RCSB PDB 1Q04 · PDBe 1Q04 · UniProt P05230

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