Structure of PDB 7nup Chain D

Receptor sequence
>7nupD (length=884) Species: 9606 (Homo sapiens) [Search protein sequence]
GAFPVATNGERFPWQELRLPSVVIPLHYDLFVHPNLTSLDFVASEKIEVL
VSNATQFIILHSKDLEITNATLQSEEDSRYMKPGKELKVLSYPAHEQIAL
LVPEKLTPHLKYYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFE
PTQARMAFPCFDEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLE
DHFETTVKMSTYLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYAL
QASLKLLDFYEKYFDIYYPLSKLDLIAIPDFAPGAMENWGLITYRETSLL
FDPKTSSASDKLWVTRVIAHELAHQWFGNLVTMEWWNDIWLNEGFAKYME
LIAVNATYPELQFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMF
DEVSYNKGACILNMLKDFLGEEKFQKGIIQYLKKFSYRNAKNDDLWSSLS
NSNAEVKEMMTTWTLQKGIPLLVVKQDGCSLRLQQERFLQGVFQEDPEWR
ALQERYLWHIPLTYSTSSSNVIHRHILKSKTDTLDLPEKTSWVKFNVDSN
GYYIVHYEGHGWDQLITQLNQNHTLLRPKDRVGLIHDVFQLVGAGRLTLD
KALDMTYYLQHETSSPALLEGLSYLESFYHMMDRRNISDISENLKRYLLQ
YFKPVIDRQSWSDKGSVWDRMLRSALLKLACDLNHAPCIQKAAELFSQWM
ESSGKLNIPTDVLKIVYSVGAQTTAGWNYLLEQYELSMSSAEQNKILYAL
STSKHQEKLLKLIELGMEGKVIKTQNLAALLHAIARRPKGQQLAWDFVRE
NWTHLLKKFDLGSYDIRMIISGTTAHFSSKDKLQEVKLFFESLEAQGSHL
DIFQTVLETITKNIKWLEKNLPTLRTWLMVNTRH
3D structure
PDB7nup Endoplasmic reticulum aminopeptidase 2 complexed with a mixed hydroxamic and sulfonyl ligand
ChainD
Resolution3.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.11.-
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 D H370 H374 E393 H320 H324 E343
BS02 USK D G334 E337 R345 W363 H370 E371 H374 E393 F450 Y455 Y892 G284 E287 R295 W313 H320 E321 H324 E343 F400 Y405 Y814
Gene Ontology
Molecular Function
GO:0004175 endopeptidase activity
GO:0004177 aminopeptidase activity
GO:0005515 protein binding
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0042277 peptide binding
GO:0046872 metal ion binding
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0002250 adaptive immune response
GO:0002474 antigen processing and presentation of peptide antigen via MHC class I
GO:0006508 proteolysis
GO:0008217 regulation of blood pressure
GO:0019885 antigen processing and presentation of endogenous peptide antigen via MHC class I
GO:0043171 peptide catabolic process
Cellular Component
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0005783 endoplasmic reticulum
GO:0005788 endoplasmic reticulum lumen
GO:0005789 endoplasmic reticulum membrane
GO:0016020 membrane

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:7nup, PDBe:7nup, PDBj:7nup
PDBsum7nup
PubMed
UniProtQ6P179|ERAP2_HUMAN Endoplasmic reticulum aminopeptidase 2 (Gene Name=ERAP2)

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