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Crystal structure of acinetobacter baumannii fabg at 1.66 a resolution

Analyse Crystal structure of acinetobacter baumannii fabg at 1.66 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6T60
Type: protein
Length: 484 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-oxoacyl-(acyl-carrier-protein) reductase
EC: 1.1.1.100
UniProt: V5VHN7
Pockets: 4 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 52% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-oxoacyl-(acyl-carrier-protein) reductase (EC 1.1.1.100)	protein	244	52% helix, 17% strand	V5VHN7
B	3-oxoacyl-(acyl-carrier-protein) reductase (EC 1.1.1.100)	protein	240	53% helix, 17% strand	V5VHN7

Pockets

4 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	541	0.70	0.79	49	empty
2	536	0.69	0.79	51	empty
3	106	0.48	0.80	13	empty
4	108	0.39	0.76	19	empty

Interfaces

1 interface between chains.

A–B · 1587 Å² buried · 31 hydrogen bonds · protein-protein

Compared structures

6T60 · Crystal structure of Acinetobacter baumannii FabG at 1.66 A resolution · 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 V5VHN7
Elsewhere: RCSB PDB 6T60 · PDBe 6T60 · UniProt V5VHN7

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