Research workbench

The 0.83 angstrom X-ray structure of the human heart fatty acid-binding protein complexed with nervonic acid

Analyse The 0.83 angstrom X-ray structure of the human heart fatty acid-binding protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7WF0
Type: protein
Length: 133 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 0.83
Source: Homo sapiens
Molecule: Fatty acid-binding protein, heart
UniProt: P05413
Ligands: NER
Pockets: 1 · best druggability 0.80

Structure

x-ray diffraction · resolution 0.83 · 1 distinct chain · 13% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fatty acid-binding protein, heart	protein	133	13% helix, 58% strand	P05413

Ligands and binding sites

NER · (15E)-tetracos-15-enoic acid · ligand · chains A
P6G · Hexaethylene glycol · 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	357	0.80	0.89	36	NER

Compared structures

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 7WF0 · PDBe 7WF0 · UniProt P05413

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.