Structure of PDB 4zla Chain B

Receptor sequence
>4zlaB (length=482) Species: 85962 (Helicobacter pylori 26695) [Search protein sequence]
MLKIKLEKTTFENAKAECSLVFIINKDFSHAWVKNKELLETFKYEGEGVF
LDQENKILYAGVKEDDVHLLRESACLAVRTLKKLAFKSVKVGVYTCGAAL
LENLKALFLGLKLGLYEYDTFKSNKKESVLKEAIVALELHKLEKSAKEAL
KYAEIMTESLNIVKDLVNTPPMIGTPVYMAEVAQKVAKENHLEIHVHDEK
FLEEKKMNAFLAVNKASLSVNPPRLIHLVYKPKKAKKKIALVGKGLTYDC
GGLSLKPADYMVTMKADKGGGSAVIGLLNALAKLGVEAEVHGIIGATENM
IGPAAYKPDDILISKEGKSIEVRNTDAEGRLVLADCLSYAQDLNPDVIVD
FATLTGACVVGLGEFTSAIMGHNEELKNLFETSGLESGELLAKLPFNRHL
KKLIESKIADVCNISSSRYGGAITAGLFLNEFIRDEFKDKWLHIDIAGPA
YVEKEWDVNSFGASGAGVRACTAFVEELLKKA
3D structure
PDB4zla Structural basis for substrate specificity of Helicobacter pylori M17 aminopeptidase.
ChainB
Resolution1.9 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) K270 R344
Catalytic site (residue number reindexed from 1) K256 R330
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 B K258 D263 D281 E342 K244 D249 D267 E328
BS02 ZN B D263 D340 E342 D249 D326 E328
BS03 NA B A461 G462 Y465 A447 G448 Y451
BS04 BCT B A341 E342 G343 R344 L368 A327 E328 G329 R330 L354
BS05 BES B K258 D263 D281 D340 E342 T367 L368 T369 G370 A461 K244 D249 D267 D326 E328 T353 L354 T355 G356 A447 MOAD: ic50=49.9nM
PDBbind-CN: -logKd/Ki=7.30,IC50=49.9nM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4zla, PDBe:4zla, PDBj:4zla
PDBsum4zla
PubMed26616008
UniProtO25294|AMPA_HELPY Cytosol aminopeptidase (Gene Name=pepA)

[Back to BioLiP]