Structure of PDB 4zi6 Chain E

Receptor sequence
>4zi6E (length=483) Species: 85962 (Helicobacter pylori 26695) [Search protein sequence]
MLKIKLEKTTFENAKAECSLVFIINKDFSHAWVKNKELLETFKYEGEGVF
LDQENKILYAGVKEDDVHLLRESACLAVRTLKKLAFKSVKVGVYTCGAAL
LENLKALFLGLKLGLYEYDTFKSNKKESVLKEAIVALELHKSLEKSAKEA
LKYAEIMTESLNIVKDLVNTPPMIGTPVYMAEVAQKVAKENHLEIHVHDE
KFLEEKKMNAFLAVNKASLSVNPPRLIHLVYKPKKAKKKIALVGKGLTYD
CGGLSLKPADYMVTMKADKGGGSAVIGLLNALAKLGVEAEVHGIIGATEN
MIGPAAYKPDDILISKEGKSIEVRNTDAEGRLVLADCLSYAQDLNPDVIV
DFATLTGACVVGLGEFTSAIMGHNEELKNLFETSGLESGELLAKLPFNRH
LKKLIESKIADVCNISSSRYGGAITAGLFLNEFIRDEFKDKWLHIDIAGP
AYVEKEWDVNSFGASGAGVRACTAFVEELLKKA
3D structure
PDB4zi6 Structural basis for substrate specificity of Helicobacter pylori M17 aminopeptidase.
ChainE
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) K270 R344
Catalytic site (residue number reindexed from 1) K257 R331
Enzyme Commision number 3.4.11.1: leucyl aminopeptidase.
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 E K258 D263 D281 E342 K245 D250 D268 E329
BS02 ZN E D263 D340 E342 D250 D327 E329
BS03 BCT E A341 G343 R344 L368 A328 G330 R331 L355
BS04 NA E A461 G462 Y465 A448 G449 Y452
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0008235 metalloexopeptidase activity
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0006508 proteolysis
GO:0019538 protein metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4zi6, PDBe:4zi6, PDBj:4zi6
PDBsum4zi6
PubMed26616008
UniProtO25294|AMPA_HELPY Cytosol aminopeptidase (Gene Name=pepA)

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