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Fabp protein before hv

Analyse Fabp protein before hv in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7DZJ
Type: protein
Length: 258 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fatty acid-binding protein, liver
UniProt: P07148
Ligands: PLM
Pockets: 3 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Fatty acid-binding protein, liver	protein	129	12% helix, 57% strand	P07148

Ligands and binding sites

PLM · Palmitic acid · ligand · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	221	0.83	0.96	39	PLM
2	221	0.83	0.95	38	PLM
3	79	0.36	0.76	21	empty

Interfaces

1 interface between chains.

A–B · 736 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (nonstandard).

Compared structures

7DZJ · Fabp protein before hv · the same entry in another collection · chain A against A, TM-score 1.00
P07148 · AlphaFold monomer V2.0 prediction for fatty acid-binding protein, liver (P07148) · a predicted model of the same protein · chain B against A, TM-score 0.95

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 P07148
Elsewhere: RCSB PDB 7DZJ · PDBe 7DZJ · UniProt P07148

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