Structure of PDB 5ab0 Chain A

Receptor sequence

>5ab0A (length=910) Species: 9606 (Homo sapiens)

PVATNGERFPWQELRLPSVVIPLHYDLFVHPNLTSLDFVASEKIEVLVSN
ATQFIILHSKDLEITNATLQSEEDSRYMKPGKELKVLSYPAHEQIALLVP
EKLTPHLKYYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFEPTQ
ARMAFPCFDEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLEDHF
ETTVKMSTYLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYALQAS
LKLLDFYEKYFDIYYPLSKLDLIAIPDFAPGAMENWGLITYRETSLLFDP
KTSSASDKLWVTRVIAHELAHQWFGNLVTMEWWNDIWLNEGFAKYMELIA
VNATYPELQFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMFDEV
SYNKGACILNMLKDFLGEEKFQKGIIQYLKKFSYRNAKNDDLWSSLSNSC
LESDFTSGGVCHSDPKMTSNMLAFLGENAEVKEMMTTWTLQKGIPLLVVK
QDGCSLRLQQERFLQGVFQEDPEWRALQERYLWHIPLTYSTSSSNVIHRH
ILKSKTDTLDLPEKTSWVKFNVDSNGYYIVHYEGHGWDQLITQLNQNHTL
LRPKDRVGLIHDVFQLVGAGRLTLDKALDMTYYLQHETSSPALLEGLSYL
ESFYHMMDRRNISDISENLKRYLLQYFKPVIDRQSWSDKGSVWDRMLRSA
LLKLACDLNHAPCIQKAAELFSQWMESSGKLNIPTDVLKIVYSVGAQTTA
GWNYLLEQYELSMSSAEQNKILYALSTSKHQEKLLKLIELGMEGKVIKTQ
NLAALLHAIARRPKGQQLAWDFVRENWTHLLKKFDLGSYDIRMIISGTTA
HFSSKDKLQEVKLFFESLEAQGSHLDIFQTVLETITKNIKWLEKNLPTLR
TWLMVNTRHH

3D structure

• PDB: 5ab0 Structural Basis for Antigenic Peptide Recognition and Processing by Endoplasmic Reticulum (Er) Aminopeptidase 2.
• Chain: A
• Resolution: 2.5 Å

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	A	E200 P201 G334 A335 E337 R345 W363 V367 H370 E371 H374 E393 F450 Y455 K756 K792 N822 L825 A857 R864 Y892 M896	E147 P148 G281 A282 E284 R292 W310 V314 H317 E318 H321 E340 F397 Y402 K703 K739 N769 L772 A804 R811 Y839 M843
BS02	BMA	A	S273 L274 R293	S220 L221 R240
BS03	ZN	A	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

External links

• PDB: RCSB:5ab0, PDBe:5ab0, PDBj:5ab0
• PDBsum: 5ab0
• PubMed: 26381406
• UniProt: Q6P179|ERAP2_HUMAN Endoplasmic reticulum aminopeptidase 2 (Gene Name=ERAP2)