MolNFT v1 · #9147 · protein

1.4 ångströms structural studies on human muscle fatty acid binding protein: binding interactions with three saturated and unsaturated C18 fatty acids

1HMS: “1.4 ångströms structural studies on human muscle fatty acid binding protein: binding interactions with three…”. X-ray diffraction, 1 ligand (OLA), 1 pocket (best druggability 0.83). MolNFT v1 #9147 on GenesisL1: 3D structure…

PDB: 1HMS
Type: protein
Length: 131 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Muscle fatty acid binding protein
UniProt: P05413
Ligands: OLA
Pockets: 1 · best druggability 0.83

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Muscle fatty acid binding protein	protein	131	13% helix, 58% strand	P05413

Ligands and binding sites

OLA · Oleic acid · ligand · 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	368	0.83	0.92	35	OLA

Compared structures

1HMS · 1.4 ångströms structural studies on human muscle fatty acid binding protein: binding… · 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 1HMS · PDBe 1HMS · UniProt P05413

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