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X-ray crystal structure of a putative acetoacyl-CoA reductase from burkholderia cenocepacia

Analyse X-ray crystal structure of a putative acetoacyl-CoA reductase from burkholderia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4K6C
Type: protein
Length: 490 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetoacetyl-CoA reductase
EC: 1.1.1.36
UniProt: B4EAU4
Ligands: CL
Pockets: 3 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Acetoacetyl-CoA reductase (EC 1.1.1.36)	protein	245	51% helix, 16% strand	B4EAU4

Ligands and binding sites

CL · Chloride ion · ion · chains A
EDO · 1,2-ethanediol · additive · 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	495	0.65	0.77	45	CL
2	430	0.61	0.76	45	empty
3	254	0.57	0.79	33	empty

Interfaces

1 interface between chains.

A–B · 1627 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

4K6C · X-ray crystal structure of a putative Acetoacyl-CoA reductase from Burkholderia… · the same entry in another collection · chain A against A, TM-score 1.00

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 B4EAU4
Elsewhere: RCSB PDB 4K6C · PDBe 4K6C · UniProt B4EAU4

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