MolNFT v1 · #166585 · protein

Crystal structure of a high molecular weight 3-oxoacyl-acp reductase (fabg) from acinetobacter baumannii crystal form 2

6UUT · 3-ketoacyl-acp reductase: “Crystal structure of a high molecular weight 3-oxoacyl-acp reductase (fabg) from acinetobacter baumannii…”. X-ray diffraction, 9 pockets (best druggability 0.78). MolNFT v1 #166585 on GenesisL1: 3D…

PDB: 6UUT
Type: protein
Length: 892 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-ketoacyl-acp reductase
EC: 1.1.1.100
UniProt: A0A219C8F5
Pockets: 9 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-ketoacyl-acp reductase (EC 1.1.1.100)	protein	460	42% helix, 18% strand	A0A219C8F5
B	3-ketoacyl-acp reductase (EC 1.1.1.100)	protein	432	41% helix, 19% strand	A0A219C8F5

Pockets

9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	984	0.78	0.80	51	empty
2	1085	0.78	0.79	69	empty
3	507	0.68	0.78	55	empty
4	117	0.61	0.87	29	empty
5	113	0.61	0.87	31	empty

Interfaces

1 interface between chains.

A–B · 3171 Å² buried · 40 hydrogen bonds · protein-protein

Compared structures

6UUT · Crystal structure of a high molecular weight 3-oxoacyl-ACP reductase (FabG) from… · 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 A0A219C8F5
Elsewhere: RCSB PDB 6UUT · PDBe 6UUT · UniProt A0A219C8F5

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