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Toward changing specificity: adipocyte lipid binding protein mutant, oleic acid bound form

Analyse Toward changing specificity: adipocyte lipid binding protein mutant, oleic acid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1G74
Type: protein
Length: 131 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adipocyte lipid-binding protein
UniProt: P04117
Ligands: OLA, PO4
Pockets: 1 · best druggability 0.84

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adipocyte lipid-binding protein	protein	131	13% helix, 59% strand	P04117

Ligands and binding sites

OLA · Oleic acid · ligand · chains A
PO4 · Phosphate ion · ion · 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	252	0.84	0.96	35	OLA

Compared structures

1G74 · Toward changing specificity: adipocyte lipid binding protein mutant, oleic acid bound form · the same entry in another collection · chain A against A, TM-score 1.00
P04117 · AlphaFold monomer V2.0 prediction for fatty acid-binding protein, adipocyte (P04117) · 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 P04117
Elsewhere: RCSB PDB 1G74 · PDBe 1G74 · UniProt P04117

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