Structure of PDB 3ctz Chain A

Receptor sequence
>3ctzA (length=617) Species: 9606 (Homo sapiens) [Search protein sequence]
PKVTSELLRQLRQAMRNSEYVTEPIQAYIIPSGDAHQSEYIAPCDCRRAF
VSGFDGSAGTAIITEEHAAMWTDGRYFLQAAKQMDSNWTLMKMGLKDTPT
QEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAGHHLIPVKENLVD
KIWTDRPERPCKPLLTLGLDYTGISWKDKVADLRLKMAERNVMWFVVTAL
DEIAWLFNLRGSDVEHNPVFFSYAIIGLETIMLFIDGDRIDAPSVKEHLL
LDLGLEAEYRIQVHPYKSILSELKALCADLSPREKVWVSDKASYAVSETI
PKDHRCCMPYTPICIAKAVKNSAESEGMRRAHIKDAVALCELFNWLEKEV
PKGGVTEISAADKAEEFRRQQADFVDLSFPTISSTGPTGAIIHYAPVPET
NRTLSLDEVYLIDSGAQYKDGTTDVTRTMHFETPTAYEKECFTYVLKGHI
AVSAAVFPTGTKGHLLDSFARSALWDSGLDYLHGTGHGVGSFLNVHEGPC
GISYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPVKTKYNFN
NRGSLTLEPLTLVPIQTKMIDVDSLTDKECDWLNNYHLTCRDVIGKELQK
QGRQEALEWLIRETQPI
3D structure
PDB3ctz Structure of human cytosolic X-prolyl aminopeptidase: a double Mn(II)-dependent dimeric enzyme with a novel three-domain subunit
ChainA
Resolution1.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.11.9: Xaa-Pro 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 MN A D426 H489 E523 E537 D424 H487 E521 E535
BS02 MN A F381 D415 D426 E537 F379 D413 D424 E535
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0008237 metallopeptidase activity
GO:0030145 manganese ion binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0006508 proteolysis
GO:0010815 bradykinin catabolic process
GO:0043069 negative regulation of programmed cell death
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3ctz, PDBe:3ctz, PDBj:3ctz
PDBsum3ctz
PubMed18515364
UniProtQ9NQW7|XPP1_HUMAN Xaa-Pro aminopeptidase 1 (Gene Name=XPNPEP1)

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