MolNFT v1 · #24091 · protein

Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with N-butyrate

1UK7 · 2-hydroxy-6-oxo-7-methylocta-2,4-dienoate hydrolase: “Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with N-butyrate”. X-ray diffraction, 1 ligand (BUA), 1 pocket (best druggability 0.76). MolNFT v1 #24091…

PDB: 1UK7
Type: protein
Length: 271 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2-hydroxy-6-oxo-7-methylocta-2,4-dienoate hydrolase
EC: 3.7.1.9
UniProt: P96965
Ligands: BUA
Pockets: 1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	2-hydroxy-6-oxo-7-methylocta-2,4-dienoate hydrolase (EC 3.7.1.9)	protein	271	42% helix, 18% strand	P96965

Ligands and binding sites

BUA · butanoic acid · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	230	0.76	0.89	41	BUA

Compared structures

1UK7 · Crystal structure of a meta-cleavage product hydrolase (CumD) complexed with n-butyrate · 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 P96965
Elsewhere: RCSB PDB 1UK7 · PDBe 1UK7 · UniProt P96965

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