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The 0.98 ångström structure of the human FABP3 Y19F mutant complexed with palmitic acid

Analyse The 0.98 ångström structure of the human FABP3 Y19F mutant complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7V2G
Type: protein
Length: 133 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fatty acid-binding protein, heart
UniProt: P05413
Ligands: PLM
Pockets: 1 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fatty acid-binding protein, heart	protein	133	14% helix, 58% strand	P05413

Ligands and binding sites

PLM · Palmitic acid · ligand · chains A
P6G · Hexaethylene glycol · additive · 2 copies · 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	311	0.83	0.93	36	PLM

Compared structures

7V2G · The 0.98 angstrom structure of the human FABP3 Y19F mutant complexed with palmitic acid · the same entry in another collection · chain A against A, TM-score 1.00
P05413 · AlphaFold monomer V2.0 prediction for fatty acid-binding protein, heart (P05413) · 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 P05413
Elsewhere: RCSB PDB 7V2G · PDBe 7V2G · UniProt P05413

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