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Crystal structure analysis of a mutant beta-ketoacyl-[acyl carrier protein] synthase II from streptococcus pneumoniae

Analyse Crystal structure analysis of a mutant beta-ketoacyl-[acyl carrier protein]… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ALM
Type: protein
Length: 412 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-oxoacyl-(acyl-carrier-protein) synthase II
EC: 2.3.1.41
UniProt: Q9FBC2
Ligands: MG
Pockets: 3 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-oxoacyl-(acyl-carrier-protein) synthase II (EC 2.3.1.41)	protein	412	37% helix, 21% strand	Q9FBC2

Ligands and binding sites

MG · Magnesium ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	94	0.55	0.85	20	empty
2	66	0.37	0.78	19	empty
3	64	0.30	0.75	14	empty

Compared structures

2ALM · Crystal structure analysis of a mutant beta-ketoacyl-[acyl carrier protein] synthase II… · 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 Q9FBC2
Elsewhere: RCSB PDB 2ALM · PDBe 2ALM · UniProt Q9FBC2

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