Structure of PDB 5ab2 Chain A Binding Site BS01

Receptor Information
>5ab2 Chain A (length=896) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PVATNGERFPWQELRLPSVVIPLHYDLFVHPNLTSLDFVASEKIEVLVSN
ATQFIILHSKDLEITNATLQSEEDSRYMKPGKELKVLSYPAHEQIALLVP
EKLTPHLKYYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFEPTQ
ARMAFPCFDEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLEDHF
ETTVKMSTYLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYALQAS
LKLLDFYEKYFDIYYPLSKLDLIAIPDFAPGAMENWGLITYRETSLLFDP
KTSSASDKLWVTRVIAHELAHQWFGNLVTMEWWNDIWLKEGFAKYMELIA
VNATYPELQFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMFDEV
SYNKGACILNMLKDFLGEEKFQKGIIQYLKKFSYRNAKNDDLWSSLSNSH
SDPKMTSNMLAFLGENAEVKEMMTTWTLQKGIPLLVVKQDGCSLRLQQER
FLQGVFQEDPEWRALQERYLWHIPLTYSTSSSNVIHRHILKSKTDTLDLP
EKTSWVKFNVDSNGYYIVHYEGHGWDQLITQLNQNHTLLRPKDRVGLIHD
VFQLVGAGRLTLDKALDMTYYLQHETSSPALLEGLSYLESFYHMMDRRNI
SDISENLKRYLLQYFKPVIDRQSWSDKGSVWDRMLRSALLKLACDLNHAP
CIQKAAELFSQWMESSGKLNIPTDVLKIVYSVGAQTTAGWNYLLEQYELS
MSSAEQNKILYALSTSKHQEKLLKLIELGMEGKVIKTQNLAALLHAIARR
PKGQQLAWDFVRENWTHLLKKFDLGSYDIRMIISGTTAHFSSKDKLQEVK
LFFESLEAQGSHLDIFQTVLETITKNIKWLEKNLPTLRTWLMVNTR
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB5ab2 Structural Basis for Antigenic Peptide Recognition and Processing by Endoplasmic Reticulum (Er) Aminopeptidase 2.
Resolution2.729 Å
Binding residue
(original residue number in PDB)		E200 G334 A335 E337 T347 W363 H370 E371 H374 E393 F450 D451 Y455 N822
Binding residue
(residue number reindexed from 1)		E147 G281 A282 E284 T294 W310 H317 E318 H321 E340 F397 D398 Y402 N757
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.-
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:5ab2, PDBe:5ab2, PDBj:5ab2
PDBsum5ab2
PubMed26381406
UniProtQ6P179|ERAP2_HUMAN Endoplasmic reticulum aminopeptidase 2 (Gene Name=ERAP2)

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