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Crystal structure of kas III from acinetobacter baumannii

Analyse Crystal structure of kas III from acinetobacter baumannii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5YZU
Type: protein
Length: 734 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-oxoacyl-[acyl-carrier-(acp)] synthase III C terminal family protein
EC: 2.3.1.180, 2.3.1.41
UniProt: V5VGF8
Pockets: 10 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-oxoacyl-[acyl-carrier-(acp)] synthase III C terminal family protein (EC 2.3.1.180, 2.3.1.41)	protein	368	40% helix, 25% strand	V5VGF8
B	3-oxoacyl-[acyl-carrier-(acp)] synthase III C terminal family protein (EC 2.3.1.180, 2.3.1.41)	protein	366	40% helix, 24% strand	V5VGF8

Pockets

10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	121	0.79	0.98	23	empty
2	267	0.67	0.83	47	empty
3	174	0.66	0.85	36	empty
4	50	0.62	0.94	21	empty
5	175	0.42	0.73	38	empty

Interfaces

1 interface between chains.

A–B · 3405 Å² buried · 66 hydrogen bonds · protein-protein

Compared structures

5YZU · Crystal structure of KAS III from Acinetobacter baumannii · 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 V5VGF8
Elsewhere: RCSB PDB 5YZU · PDBe 5YZU · UniProt V5VGF8

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