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Enoyl-acp reducatase fabv from burkholderia pseudomallei (apo)

Analyse Enoyl-acp reducatase fabv from burkholderia pseudomallei (apo) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4BKO
Type: protein
Length: 404 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative reductase BURPS305_1051
EC: 1.3.1.9
UniProt: A4MGI8
Ligands: SO4
Pockets: 4 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative reductase BURPS305_1051 (EC 1.3.1.9)	protein	404	41% helix, 18% strand	A4MGI8

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A
GOL · Glycerol · additive · 3 copies · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A

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

Pockets

4 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	995	0.83	0.84	79	MES, GOL
2	72	0.39	0.79	18	empty
3	52	0.36	0.79	13	empty
4	58	0.29	0.74	12	empty

Compared structures

4BKO · Enoyl-ACP reducatase FabV from Burkholderia pseudomallei (apo) · 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 A4MGI8
Elsewhere: RCSB PDB 4BKO · PDBe 4BKO · UniProt A4MGI8

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