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Crystal structure of C16T/K12V/C117V/P134V mutant of human acidic fibroblast growth factor

Analyse Crystal structure of C16T/K12V/C117V/P134V mutant of human acidic fibroblast… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4Q9P
Type: protein
Length: 271 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fibroblast growth factor 1
UniProt: P05230
Pockets: 2 · best druggability 0.53

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fibroblast growth factor 1	protein	131	11% helix, 41% strand	P05230
B	Fibroblast growth factor 1	protein	140	6% helix, 37% strand	P05230

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	175	0.53	0.79	34	empty
2	110	0.40	0.76	28	empty

Interfaces

1 interface between chains.

A–B · 807 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

4Q9P · Crystal structure of C16T/K12V/C117V/P134V mutant of human acidic fibroblast growth factor · 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 0.98

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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 4Q9P · PDBe 4Q9P · UniProt P05230

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