Structure of PDB 4v1x Chain E

Receptor sequence
>4v1xE (length=474) Species: 47660 (Pseudomonas sp. ADP) [Search protein sequence]
MQTLSIQHGTLVTMDQYRRVLGDSWVHVQDGRIVALGVHAESVPPPADRV
IDARGKVVLPGFINAHTHVNQILLRGGPSHGRQFYDWLFNVVYPGQKAMR
PEDVAVAVRLYCAEAVRSGITTINENADSAIYPGNIEAAMAVYGEVGVRV
VYARMFFDRMDGRIQGYVDALKARSPQVELCSIMEETAVAKDRITALSDQ
YHGTAGGRISVWPAPATTTAVTVEGMRWAQAFARDRAVMWTLHMAESDHD
ERIHGMSPAEYMECYGLLDERLQVAHCVYFDRKDVRLLHRHNVKVASQVV
SNAYLGSGVAPVPEMVERGMAVGIGTDNGNSNDSVNMIGDMKFMAHIHRA
VHRDADVLTPEKILEMATIDGARSLGMDHEIGSIETGKRADLILLDLRHP
QTTPHHHLAATIVFQAYGNEVDTVLIDGNVVMENRRLSFLPPERELAFLE
EAQSRATAILQRANMVANPAWRSL
3D structure
PDB4v1x The Structure of the Hexameric Atrazine Chlorohydrolase Atza.
ChainE
Resolution2.2 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 3.8.1.8: atrazine chlorohydrolase.
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 FE E H66 H68 H243 H276 D327 H66 H68 H243 H276 D327
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
GO:0018788 atrazine chlorohydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0019381 atrazine catabolic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4v1x, PDBe:4v1x, PDBj:4v1x
PDBsum4v1x
PubMed25760618
UniProtP72156|ATZA_PSESD Atrazine chlorohydrolase (Gene Name=atzA)

[Back to BioLiP]