Structure of PDB 2qt3 Chain B

Receptor sequence

>2qt3B (length=401) Species: 47660 (Pseudomonas sp. ADP)

KDFDLIIRNAYLSEKDSVYDIGIVGDRIIKIEAKIEGTVKDEIDAKGNLV
SPGFVDAHTHMDKSFTSTGERLPKFWSRPYTRDAAIEDGLKYYKNATHEE
IKRHVIEHAHMQVLHGTLYTRTHVDVDSVAKTKAVEAVLEAKEELKDLID
IQVVAFAQSGFFVDLESESLIRKSLDMGCDLVGGVDPATRENNVEGSLDL
CFKLAKEYDVDIDYHIHDIGTVGVYSINRLAQKTIENGYKGRVTTSHAWC
FADAPSEWLDEAIPLYKDSGMKFVTCFSSTPPTMPVIKLLEAGINLGCAS
DNIRDFWVPFGNGDMVQGALIETQRLELKTNRDLGLIWKMITSEGARVLG
IEKNYGIEVGKKADLVVLNSLSPQWAIIDQAKRLCVIKNGRIIVKDEVIV
A

3D structure

• PDB: 2qt3 Crystal structure of N-Isopropylammelide isopropylaminohydrolase AtzC from Pseudomonas sp. strain ADP complexed with Zn.
• Chain: B
• Resolution: 2.24 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H60 H62 Q160 H217 D220 D303
• Catalytic site (residue number reindexed from 1): H58 H60 Q158 H215 D218 D301
• 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	H58 H60 H215

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:2qt3, PDBe:2qt3, PDBj:2qt3
• PDBsum: 2qt3
• UniProt: O52063|ATZC_PSESD N-isopropylammelide isopropyl amidohydrolase (Gene Name=atzC)