Structure of PDB 4cqb Chain A

Receptor sequence

>4cqbA (length=402) Species: 47660 (Pseudomonas sp. ADP)

SKDFDLIIRNAYLSEKDSVYDIGIVGDRIIKIEAKIEGTVKDEIDAKGNL
VSPGFVDAHTHMDKSFTSTGERLPKFWSRPYTRDAAIEDGLKYYKNATHE
EIKRHVIEHAHMQVLHGTLYTRTHVDVDSVAKTKAVEAVLEAKEELKDLI
DIQVVAFAQSGFFVDLESESLIRKSLDMGCDLVGGVDPATRENNVEGSLD
LCFKLAKEYDVDIDYHIHDIGTVGVYSINRLAQKTIENGYKGRVTTSHAW
CFADAPSEWLDEAIPLYKDSGMKFVTCFSSTPPTMPVIKLLEAGINLGCA
SDNIRDFWVPFGNGDMVQGALIETQRLELKTNRDLGLIWKMITSEGARVL
GIEKNYGIEVGKKADLVVLNSLSPQWAIIDQAKRLCVIKNGRIIVKDEVI
VA

3D structure

• PDB: 4cqb X-Ray Structure and Mutagenesis Studies of the N-Isopropylammelide Isopropylaminohydrolase, Atzc
• Chain: A
• Resolution: 1.84 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H60 H62 Q160 H217 D220 D303
• Catalytic site (residue number reindexed from 1): H59 H61 Q159 H216 D219 D302
• Enzyme Commision number: 3.5.4.42: N-isopropylammelide isopropylaminohydrolase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	ZN	A	H60 H62 H217 D303	H59 H61 H216 D302

Gene Ontology

Molecular Function

• GO:0016787 hydrolase activity
• GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
• GO:0016814 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
• GO:0018764 N-isopropylammelide isopropylaminohydrolase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0019381 atrazine catabolic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:4cqb, PDBe:4cqb, PDBj:4cqb
• PDBsum: 4cqb
• PubMed: 26390431
• UniProt: O52063|ATZC_PSESD N-isopropylammelide isopropyl amidohydrolase (Gene Name=atzC)