Structure of PDB 3se6 Chain B

Receptor sequence
>3se6B (length=859) Species: 9606 (Homo sapiens) [Search protein sequence]
VATNGERFPWQELRLPSVVIPLHYDLFVHPNLTSLDFVASEKIEVLVSNA
TQFIILHSKDLEITNATLQSEPGKELKVLSYPAHEQIALLVPEKLTPHLK
YYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFEPTQARMAFPCF
DEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLEDHFETTVKMST
YLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYALQASLKLLDFYE
KYFDIYYPLSKLDLIAIPDFAPGAMENWGLITYRETSLLFDPKTSSASDK
LWVTRVIAHELAHQWFGNLVTMEWWNDIWLNEGFAKYMELIAVNATYPEL
QFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMFDEVSYNKGACI
LNMLKDFLGEEKFQKGIIQYLKKFSYRNAKNDDLWSSLSNSAEVKEMMTT
WTLQKGIPLLVVKQDGCSLRLQQERFLQGVRYLWHIPLTYSTSSSNVIHR
HILKSKTDTLDLPEKTSWVKFNVDSNGYYIVHYEGHGWDQLITQLNQNHT
LLRPKDRVGLIHDVFQLVGAGRLTLDKALDMTYYLQHETSSPALLEGLSY
LESFYHMMDRRNISDISENLKRYLLQYFKPVIDRQSWSDKGSVWDRMLRS
ALLKLACDLNHAPCIQKAAELFSQWMESSGKLNIPTDVLKIVYSVGAQTT
AGWNYLLEQYELSMSSAEQNKILYALSTSKHQEKLLKLIELGMEGKVIKT
QNLAALLHAIARRPKGQQLAWDFVRENWTHLLKKFDLGSYDIRMIISGTT
AHFSSKDKLQEVKLFFESLEAQGSHLDIFQTVLETITKNIKWLEKNLPTL
RTWLMVNTR
3D structure
PDB3se6 The crystal structure of human endoplasmic reticulum aminopeptidase 2 reveals the atomic basis for distinct roles in antigen processing.
ChainB
Resolution3.08 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E337 H370 E371 H374 E393 Q447 Y455
Catalytic site (residue number reindexed from 1) E276 H309 E310 H313 E332 Q386 Y394
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 LYS B E200 P333 M336 E337 H370 E371 H374 E393 Y455 E139 P272 M275 E276 H309 E310 H313 E332 Y394
BS02 ZN B H370 H374 E393 H309 H313 E332
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:3se6, PDBe:3se6, PDBj:3se6
PDBsum3se6
PubMed22106953
UniProtQ6P179|ERAP2_HUMAN Endoplasmic reticulum aminopeptidase 2 (Gene Name=ERAP2)

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