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Crystal structure of acbp from armadillo harderian gland

Analyse Crystal structure of acbp from armadillo harderian gland in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FDQ
Type: protein
Length: 258 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acyl-CoA-binding protein
UniProt: P82934
Pockets: 3 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 65% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Acyl-CoA-binding protein	protein	86	65% helix, 0% strand	P82934

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	435	0.67	0.79	45	empty
2	173	0.45	0.74	27	empty
3	179	0.44	0.74	26	empty

Interfaces

3 interfaces between chains.

A–C · 591 Å² buried · 1 hydrogen bond · protein-protein
A–B · 560 Å² buried · 0 hydrogen bonds · protein-protein
B–C · 16 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2FDQ · crystal structure of ACBP from Armadillo Harderian Gland · the same entry in another collection · chain A against A, TM-score 1.00
P82934 · AlphaFold monomer V2.0 prediction for acyl-CoA-binding protein (P82934) · a predicted model of the same protein · chain C against A, TM-score 0.98

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 P82934
Elsewhere: RCSB PDB 2FDQ · PDBe 2FDQ · UniProt P82934

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