Structure of PDB 5t13 Chain A

Receptor sequence
>5t13A (length=376) Species: 550 (Enterobacter cloacae) [Search protein sequence]
HHHHHHMQAQVFRVPMSNPADVSGVAKLIDEGVIRAEEVVCVLGKTEGNG
CVNDFTRGYTTLAFKVYFSEKLGVSRQEVGERIAFIMSGGTEGVMAPHCT
IFTVQKTDNKQKTAAEGKRLAVQQIFTREFLPEEIGRMPQVTETADAVRR
AMREAGIADASDVHFVQVKCPLLTAGRMHDAVERGHTVATEDTYESMGYS
RGASALGIALALGEVEKANLSDEVITADYSLYSSVASTSAGIELMNNEII
VMGNSRAWGGDLVIGHAEMKDAIDGAAVRQALRDVGCCENDLPTVDELGR
VVNVFAKAEASPDGEVRNRRHTMLDDSDINSTRHARAVVNAVIASIVGDP
MVYVSGGSEHQGPAGGGPVAVIARTA
3D structure
PDB5t13 Structure of the Cyanuric Acid Hydrolase TrzD Reveals Product Exit Channel.
ChainA
Resolution2.19 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.5.2.15: cyanuric acid amidohydrolase.
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 CO2 A S82 G83 S233 R330 S349 G350 S88 G89 S239 R336 S355 G356
BS02 CO2 A R51 G235 I236 E237 R57 G241 I242 E243
BS03 MG A E303 S352 Q355 G356 P357 G360 E309 S358 Q361 G362 P363 G366
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0016812 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
GO:0018753 cyanuric acid amidohydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0019381 atrazine catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5t13, PDBe:5t13, PDBj:5t13
PDBsum5t13
PubMed28345631
UniProtP0A3V4|CAH_ENTCL Cyanuric acid amidohydrolase (Gene Name=trzD)

[Back to BioLiP]