Structure of PDB 4e36 Chain A

Receptor sequence
>4e36A (length=869) Species: 9606 (Homo sapiens) [Search protein sequence]
PVATNGERFPWQELRLPSVVIPLHYDLFVHPNLTSLDFVASEKIEVLVSN
ATQFIILHSKDLEITNATLQSEEYMKPGKELKVLSYPAHEQIALLVPEKL
TPHLKYYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFEPTQARM
AFPCFDEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLEDHFETT
VKMSTYLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYALQASLKL
LDFYEKYFDIYYPLSKLDLIAIPDFAPGAMENWGLITYRETSLLFDPKTS
SASDKLWVTRVIAHELAHQWFGNLVTMEWWNDIWLKEGFAKYMELIAVNA
TYPELQFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMFDEVSYN
KGACILNMLKDFLGEEKFQKGIIQYLKKFSYRNAKNDDLWSSLSNSLGEN
AEVKEMMTTWTLQKGIPLLVVKQDGCSLRLQQERFLQGQERYLWHIPLTY
STSSSNVIHRHILKSKTDTLDLPEKTSWVKFNVDSNGYYIVHYEGHGWDQ
LITQLNQNHTLLRPKDRVGLIHDVFQLVGAGRLTLDKALDMTYYLQHETS
SPALLEGLSYLESFYHMMDRRNISDISENLKRYLLQYFKPVIDRQSWSDK
GSVWDRMLRSALLKLACDLNHAPCIQKAAELFSQWMESSGKLNIPTDVLK
IVYSVGAQTTAGWNYLLEQYELSMSSAEQNKILYALSTSKHQEKLLKLIE
LGMEGKVIKTQNLAALLHAIARRPKGQQLAWDFVRENWTHLLKKFDLGSY
DIRMIISGTTAHFSSKDKLQEVKLFFESLEAQGSHLDIFQTVLETITKNI
KWLEKNLPTLRTWLMVNTR
3D structure
PDB4e36 A common single nucleotide polymorphism in endoplasmic reticulum aminopeptidase 2 induces a specificity switch that leads to altered antigen processing.
ChainA
Resolution3.22 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) E281 H314 E315 H318 E337 Q391 Y399
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 A D198 E200 P333 A335 E337 H370 E371 H374 Y455 D142 E144 P277 A279 E281 H314 E315 H318 Y399
BS02 ZN A H370 H374 E393 H314 H318 E337
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:4e36, PDBe:4e36, PDBj:4e36
PDBsum4e36
PubMed22837489
UniProtQ6P179|ERAP2_HUMAN Endoplasmic reticulum aminopeptidase 2 (Gene Name=ERAP2)

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