Structure of PDB 5ab2 Chain B

Receptor sequence
>5ab2B (length=878) Species: 9606 (Homo sapiens) [Search protein sequence]
PVATNGERFPWQELRLPSVVIPLHYDLFVHPNLTSLDFVASEKIEVLVSN
ATQFIILHSKDLEITNATLQSEEDSRYMKPGKELKVLSYPAHEQIALLVP
EKLTPHLKYYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFEPTQ
ARMAFPCFDEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLEDHF
ETTVKMSTYLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYALQAS
LKLLDFYEKYFDIYYPLSKLDLIAIPDFAPGAMENWGLITYRETSLLFDP
KTSSASDKLWVTRVIAHELAHQWFGNLVTMEWWNDIWLKEGFAKYMELIA
VNATYPELQFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMFDEV
SYNKGACILNMLKDFLGEEKFQKGIIQYLKKFSYRNAKNDDLWSSLSNSA
EVKEMMTTWTLQKGIPLLVVKQDGCSLRLQQERFLQGVFQEDPEWRALQE
RYLWHIPLTYSTSSSNVIHRHILKSKTDTLDLPEKTSWVKFNVDSNGYYI
VHYEGHGWDQLITQLNQNHTLLRPKDRVGLIHDVFQLVGAGRLTLDKALD
MTYYLQHETSSPALLEGLSYLESFYHMMDRRNISDISENLKRYLLQYFKP
VIDRQSWSDKGSVWDRMLRSALLKLACDLNHAPCIQKAAELFSQWMESSG
KLNIPTDVLKIVYSVGAQTTAGWNYLLEQYELSMSSAEQNKILYALSTSK
HQEKLLKLIELGMEGKVIKTQNLAALLHAIARRPKGQQLAWDFVRENWTH
LLKKFDLGSYDIRMIISGTTAHFSSKDKLQEVKLFFESLEAQGSHLDIFQ
TVLETITKNIKWLEKNLPTLRTWLMVNT
3D structure
PDB5ab2 Structural Basis for Antigenic Peptide Recognition and Processing by Endoplasmic Reticulum (Er) Aminopeptidase 2.
ChainB
Resolution2.729 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) E337 H370 E371 H374 E393 Q447 Y455
Catalytic site (residue number reindexed from 1) E284 H317 E318 H321 E340 Q394 Y402
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 peptide B P333 E337 R345 D360 W363 H370 E371 H374 E393 D451 E452 Y455 Y892 P280 E284 R292 D307 W310 H317 E318 H321 E340 D398 E399 Y402 Y810
BS02 ZN B H370 H374 E393 H317 H321 E340
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5ab2, PDBe:5ab2, PDBj:5ab2
PDBsum5ab2
PubMed26381406
UniProtQ6P179|ERAP2_HUMAN Endoplasmic reticulum aminopeptidase 2 (Gene Name=ERAP2)

[Back to BioLiP]