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Crystal Structure of human FABP4 in complex with 2-(1H-indol-7-yloxymethyl)-1,3-thiazole-4-carboxylic acid

Analyse Crystal Structure of human FABP4 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7G17
Type: protein
Length: 134 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.05
Source: Homo sapiens
Molecule: Fatty acid-binding protein, adipocyte
UniProt: P15090
Ligands: WMQ, SO4
Pockets: 1 · best druggability 0.85

Structure

x-ray diffraction · resolution 1.05 · 1 distinct chain · 15% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fatty acid-binding protein, adipocyte	protein	134	15% helix, 57% strand	P15090

Ligands and binding sites

WMQ · 2-{[(1H-indol-7-yl)oxy]methyl}-1,3-thiazole-4-carboxylic acid · ligand · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A
EDO · 1,2-ethanediol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	316	0.85	0.95	33	WMQ, EDO

Compared structures

P15090 · AlphaFold monomer V2.0 prediction for fatty acid-binding protein, adipocyte (P15090) · a predicted model of the same protein · chain A 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 P15090
Elsewhere: RCSB PDB 7G17 · PDBe 7G17 · UniProt P15090

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