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The 0.88 ångström X-ray structure of the human heart fatty acid- binding protein complexed with stearic acid

Analyse The 0.88 ångström X-ray structure of the human heart fatty acid- binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WVM
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: STE
Pockets: 1 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 59% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fatty acid-binding protein, heart	protein	133	13% helix, 59% strand	P05413

Ligands and binding sites

STE · Stearic 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	314	0.83	0.93	35	STE

Compared structures

3WVM · The 0.88 angstrom X-ray structure of the human heart fatty acid-binding protein complexed… · 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 3WVM · PDBe 3WVM · UniProt P05413

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