Structure of PDB 3vh9 Chain A

Receptor sequence
>3vh9A (length=291) Species: 671 (Vibrio proteolyticus) [Search protein sequence]
MPPITQQATVTAWLPQVDASQITGTISSLESFTNRFYTTTSGAQASDWIA
SEWQALSASLPNASVKQVSHSGYNQKSVVMTITGSEAPDEWIVIGGHLDS
TIGSHTNEQSVAPGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAA
EEVGLRGSQDLANQYKSEGKNVVSALQLDMTNYKGSAQDVVFITDYTDSN
FTQYLTQLMDEYLPSLTYGFDTCGYACSDHASWHNAGYPAAMPFESKFND
YNPRIHTTQDTLANSDPTGSHAKKFTQLGLAYAIEMGSATG
3D structure
PDB3vh9 Potent inhibition of dinuclear zinc(II) peptidase, an aminopeptidase from Aeromonas proteolytica, by 8-quinolinol derivatives: inhibitor design based on Zn(2+) fluorophores, kinetic, and X-ray crystallographic study.
ChainA
Resolution1.29 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H97 D117 E151 E152 D179 H256
Catalytic site (residue number reindexed from 1) H97 D117 E151 E152 D179 H256
Enzyme Commision number 3.4.11.10: bacterial leucyl aminopeptidase.
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 A D117 E152 H256 D117 E152 H256
BS02 ZN A H97 D117 D179 H97 D117 D179
BS03 HQY A D117 E152 D179 Y225 Y251 I255 H256 D117 E152 D179 Y225 Y251 I255 H256 MOAD: Ki=0.58uM
PDBbind-CN: -logKd/Ki=6.24,Ki=0.58uM
Gene Ontology
Molecular Function
GO:0008235 metalloexopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:3vh9, PDBe:3vh9, PDBj:3vh9
PDBsum3vh9
PubMed22311113
UniProtQ01693|AMPX_VIBPR Bacterial leucyl aminopeptidase

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