Research workbench

Crystal structure of a 3-oxoacyl-acyl-carrier protein reductase FABG4 from mycobacterium smegmatis bound to NAD

Analyse Crystal structure of a 3-oxoacyl-acyl-carrier protein reductase FABG4 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5VP5
Type: protein
Length: 411 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-oxoacyl-acyl-carrier protein reductase FABG4
EC: 1.1.1.100
UniProt: A0QPE7
Ligands: NAD, CL
Pockets: 3 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-oxoacyl-acyl-carrier protein reductase FABG4 (EC 1.1.1.100)	protein	411	39% helix, 19% strand	A0QPE7

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
CL · Chloride ion · ion · 2 copies · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	127	0.67	0.89	22	empty
2	330	0.56	0.75	47	NAD
3	76	0.30	0.73	17	empty

Compared structures

5VP5 · Crystal structure of a 3-oxoacyl-acyl-carrier protein reductase FabG4 from Mycobacterium… · 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 A0QPE7
Elsewhere: RCSB PDB 5VP5 · PDBe 5VP5 · UniProt A0QPE7

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.