Structure of PDB 4cqb Chain B

Receptor sequence

>4cqbB (length=400) Species: 47660 (Pseudomonas sp. ADP)

DFDLIIRNAYLSEKDSVYDIGIVGDRIIKIEAKIEGTVKDEIDAKGNLVS
PGFVDAHTHMDKSFTSTGERLPKFWSRPYTRDAAIEDGLKYYKNATHEEI
KRHVIEHAHMQVLHGTLYTRTHVDVDSVAKTKAVEAVLEAKEELKDLIDI
QVVAFAQSGFFVDLESESLIRKSLDMGCDLVGGVDPATRENNVEGSLDLC
FKLAKEYDVDIDYHIHDIGTVGVYSINRLAQKTIENGYKGRVTTSHAWCF
ADAPSEWLDEAIPLYKDSGMKFVTCFSSTPPTMPVIKLLEAGINLGCASD
NIRDFWVPFGNGDMVQGALIETQRLELKTNRDLGLIWKMITSEGARVLGI
EKNYGIEVGKKADLVVLNSLSPQWAIIDQAKRLCVIKNGRIIVKDEVIVA

3D structure

• PDB: 4cqb X-Ray Structure and Mutagenesis Studies of the N-Isopropylammelide Isopropylaminohydrolase, Atzc
• Chain: B
• 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): H57 H59 Q157 H214 D217 D300
• 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	B	H60 H62 H217 D303	H57 H59 H214 D300

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)