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Crystal structure of N-isopropylammelide isopropylaminohydrolase from burkholderia multivorans atcc 17616

Analyse Crystal structure of N-isopropylammelide isopropylaminohydrolase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6NBO
Type: protein
Length: 390 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-isopropylammelide isopropylaminohydrolase
EC: 3.5.4.42
UniProt: A0A0H3KPJ4
Ligands: ZN, CL
Pockets: 3 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-isopropylammelide isopropylaminohydrolase (EC 3.5.4.42)	protein	390	35% helix, 23% strand	A0A0H3KPJ4

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A
CL · Chloride ion · ion · 6 copies · chains A
EDO · 1,2-ethanediol · additive · 4 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	265	0.57	0.78	40	ZN
2	70	0.34	0.76	15	empty
3	51	0.28	0.75	16	EDO

Compared structures

6NBO · Crystal structure of N-isopropylammelide isopropylaminohydrolase from Burkholderia… · 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 A0A0H3KPJ4
Elsewhere: RCSB PDB 6NBO · PDBe 6NBO · UniProt A0A0H3KPJ4

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