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Crystal structure of caib mutant D169A in complex with coenzyme a

Analyse Crystal structure of caib mutant D169A in complex with coenzyme a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XVU
Type: protein
Length: 402 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Crotonobetainyl-COA:CARNITINE CoA-transferase
EC: 2.8.3.-
UniProt: P31572
Ligands: COA
Pockets: 3 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Crotonobetainyl-COA:CARNITINE CoA-transferase (EC 2.8.3.-)	protein	402	38% helix, 17% strand	P31572

Ligands and binding sites

COA · Coenzyme A · ligand · chains A

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

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	349	0.65	0.80	39	COA
2	90	0.43	0.79	18	empty
3	137	0.42	0.75	20	empty

Compared structures

1XVU · Crystal Structure of CaiB mutant D169A in complex with Coenzyme A · the same entry in another collection · chain A against A, TM-score 1.00
P31572 · AlphaFold monomer V2.0 prediction for L-carnitine CoA-transferase (P31572) · a predicted model of the same protein · chain A 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 P31572
Elsewhere: RCSB PDB 1XVU · PDBe 1XVU · UniProt P31572

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