Structure of PDB 2iq6 Chain A

Receptor sequence
>2iq6A (length=291) Species: 671 (Vibrio proteolyticus) [Search protein sequence]
MPPITQQATVTAWLPQVDASQITGTISSLESFTNRFYTTTSGAQASDWIA
SEWQALSASLPNASVKQVSHSGYNQKSVVMTITGSEAPDEWIVIGGHLDS
TIGSHTNEQSVAPGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAA
EEVGLRGSQDLANQYKSEGKNVVSALQLDMTNYKGSAQDVVFITDYTDSN
FTQYLTQLMDEYLPSLTYGFDTCGYACSDHASWHNAGYPAAMPFESKFND
YNPRIHTTQDTLANSDPTGSHAKKFTQLGLAYAIEMGSATG
3D structure
PDB2iq6 Experimental evidence for a metallohydrolase mechanism in which the nucleophile is not delivered by a metal ion: EPR spectrokinetic and structural studies of aminopeptidase from Vibrio proteolyticus
ChainA
Resolution2.0 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 peptide A T101 D117 E151 E152 V153 D179 M180 Y225 C227 H256 T101 D117 E151 E152 V153 D179 M180 Y225 C227 H256
BS02 ZN A D117 E152 H256 D117 E152 H256
BS03 ZN A H97 D117 D179 H97 D117 D179
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:2iq6, PDBe:2iq6, PDBj:2iq6
PDBsum2iq6
PubMed17238863
UniProtQ01693|AMPX_VIBPR Bacterial leucyl aminopeptidase

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