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Crystal structure of "L44F/M67I/L73V/A103G/DELETION 104- 106/F108Y/V109L/L111I/C117V/R119G/DELETION 120-122" mutant form of human acidic fibroblast growth factor

Analyse Crystal structure of "L44F/M67I/L73V/A103G/DELETION 104… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3O3Q
Type: protein
Length: 499 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heparin-binding growth factor 1
UniProt: P05230
Pockets: 6 · best druggability 0.57

Structure

x-ray diffraction · 3 distinct chains · 4% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heparin-binding growth factor 1	protein	123	2% helix, 46% strand	P05230
B	Heparin-binding growth factor 1	protein	122	2% helix, 47% strand	P05230
C, D	Heparin-binding growth factor 1	protein	127	7% helix, 45% strand	P05230

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains B, A, D

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	57	0.57	0.90	20	GOL
2	240	0.53	0.76	27	empty
3	171	0.44	0.75	28	empty
4	56	0.42	0.82	17	empty
5	75	0.39	0.78	20	empty

Interfaces

5 interfaces between chains.

A–D · 723 Å² buried · 12 hydrogen bonds · protein-protein
A–C · 547 Å² buried · 13 hydrogen bonds · protein-protein
A–B · 530 Å² buried · 7 hydrogen bonds · protein-protein
C–D · 125 Å² buried · 2 hydrogen bonds · protein-protein
B–C · 24 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

3O3Q · Crystal structure of L44F/M67I/L73V/A103G/deletion… · the same entry in another collection · chain C against C, TM-score 1.00
P05230 · AlphaFold monomer V2.0 prediction for fibroblast growth factor 1 (P05230) · a predicted model of the same protein · chain C against A, TM-score 0.97

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 3O3Q · PDBe 3O3Q · UniProt P05230

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