Structure of PDB 7nup Chain C

Receptor sequence
>7nupC (length=883) Species: 9606 (Homo sapiens) [Search protein sequence]
AFPVATNGERFPWQELRLPSVVIPLHYDLFVHPNLTSLDFVASEKIEVLV
SNATQFIILHSKDLEITNATLQSEEDSRYMKPGKELKVLSYPAHEQIALL
VPEKLTPHLKYYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFEP
TQARMAFPCFDEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLED
HFETTVKMSTYLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYALQ
ASLKLLDFYEKYFDIYYPLSKLDLIAIPDFAPGAMENWGLITYRETSLLF
DPKTSSASDKLWVTRVIAHELAHQWFGNLVTMEWWNDIWLNEGFAKYMEL
IAVNATYPELQFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMFD
EVSYNKGACILNMLKDFLGEEKFQKGIIQYLKKFSYRNAKNDDLWSSLSN
SGENAEVKEMMTTWTLQKGIPLLVVKQDGCSLRLQQERFLQGVFQEDPEW
RALQERYLWHIPLTYSTSSSNVIHRHILKSKTDTLDLPEKTSWVKFNVDS
NGYYIVHYEGHGWDQLITQLNQNHTLLRPKDRVGLIHDVFQLVGAGRLTL
DKALDMTYYLQHETSSPALLEGLSYLESFYHMMDRRNISDISENLKRYLL
QYFKPVIDRQSWSDKGSVWDRMLRSALLKLACDLNHAPCIQKAAELFSQW
MESSGKLNIPTDVLKIVYSVGAQTTAGWNYLLEQYELSMSSAEQNKILYA
LSTSKHQEKLLKLIELGMEGKVIKTQNLAALLHAIARRPKGQQLAWDFVR
ENWTHLLKKFDLGSYDIRMIISGTTAHFSSKDKLQEVKLFFESLEAQGSH
LDIFQTVLETITKNIKWLEKNLPTLRTWLMVNT
3D structure
PDB7nup Endoplasmic reticulum aminopeptidase 2 complexed with a mixed hydroxamic and sulfonyl ligand
ChainC
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 C H370 H374 E393 H319 H323 E342
BS02 USK C G334 A335 E337 H370 E371 H374 E393 K397 F450 D451 E452 Y455 Y892 R895 G283 A284 E286 H319 E320 H323 E342 K346 F399 D400 E401 Y404 Y815 R818
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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