MolNFT v1 · #152606 · protein

Crystal structure of an acetolactate decarboxylase from klebsiella pneumoniae

6INC · Alpha-acetolactate decarboxylase: “Crystal structure of an acetolactate decarboxylase from klebsiella pneumoniae”. X-ray diffraction, 3 ligands (ZN, NA, CL), 2 pockets (best druggability 0.54). MolNFT v1 #152606 on GenesisL1: 3D…

PDB: 6INC
Type: protein
Length: 218 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-acetolactate decarboxylase
EC: 4.1.1.5
UniProt: W9BHF3
Ligands: ZN, NA, CL
Pockets: 2 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-acetolactate decarboxylase (EC 4.1.1.5)	protein	218	17% helix, 47% strand	W9BHF3

Ligands and binding sites

ZN · Zinc ion · metal · chains A
NA · Sodium ion · metal · chains A
CL · Chloride ion · ion · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 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	202	0.54	0.78	22	CL, EDO, NA
2	54	0.41	0.82	24	empty

Compared structures

6INC · Crystal structure of an acetolactate decarboxylase from Klebsiella pneumoniae · 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 W9BHF3
Elsewhere: RCSB PDB 6INC · PDBe 6INC · UniProt W9BHF3

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