Structure of PDB 4ha0 Chain A

Receptor sequence
>4ha0A (length=323) Species: 235909 (Geobacillus kaustophilus HTA426) [Search protein sequence]
EMVETVCGPVPVEQLGKTLIHEHFLFGYPGFQGDVTRGTFREDESLRVAV
EAAEKMKRHGIQTVVDPTPNDCGRNPAFLRRVAEETGLNIICATGYYYEG
EGAPPYFQFRRLLGTAEDDIYDMFMAELTEGIADTGIKAGVIKLASSKGR
ITEYEKMFFRAAARAQKETGAVIITHTQEGTMGPEQAAYLLEHGADPKKI
VIGHMCGNTDPDYHRKTLAYGVYIAFDDFGIQGMVGAPTDEERVRTLLAL
LRDGYEKQIMLSHDTVNVWLGRPFTLPEPFAEMMKNWHVEHLFVNIIPAL
KNEGIRDEVLEQMFIGNPAALFS
3D structure
PDB4ha0 Structural evidence of a productive active site architecture for an evolved quorum-quenching GKL lactonase.
ChainA
Resolution1.902 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) H23 H25 K145 H178 H206 G209 D230 D266
Catalytic site (residue number reindexed from 1) H21 H23 K143 H176 H204 G207 D228 D264
Enzyme Commision number 3.5.-.-
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 A H23 H25 K145 D266 H21 H23 K143 D264
BS02 ZN A K145 H178 H206 K143 H176 H204
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0009056 catabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:4ha0, PDBe:4ha0, PDBj:4ha0
PDBsum4ha0
PubMed23461395
UniProtQ5KZU5

[Back to BioLiP]