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Crystal structure of Arabidopsis thaliana fatty-acid binding protein At1g53520 (AtFAP3)

Analyse Crystal structure of Arabidopsis thaliana fatty-acid binding protein At1g53520… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4DOL
Type: protein
Length: 207 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.7
Source: Arabidopsis thaliana
Molecule: At1g53520
UniProt: Q9C8L2
Ligands: PLM
Pockets: 1 · best druggability 0.79

Structure

x-ray diffraction · resolution 1.7 · 1 distinct chain · 36% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	At1g53520	protein	207	36% helix, 29% strand	Q9C8L2

Ligands and binding sites

PLM · Palmitic 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	215	0.79	0.92	24	PLM

Compared structures

4DOL · Crystal structure of arabidopsis thaliana fatty-acid binding protein AT1G53520 (ATFAP3) · the same entry in another collection · chain A against A, TM-score 1.00
Q9C8L2 · AlphaFold monomer V2.0 prediction for fatty-acid-binding protein 3, chloroplastic (Q9C8L2) · 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 Q9C8L2
Elsewhere: RCSB PDB 4DOL · PDBe 4DOL · UniProt Q9C8L2

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