Structure of PDB 6ea4 Chain B

Receptor sequence
>6ea4B (length=869) Species: 9606 (Homo sapiens) [Search protein sequence]
PVATNGERFPWQELRLPSVVIPLHYDLFVHPNLTSLDFVASEKIEVLVSN
ATQFIILHSKDLEITNATLQSEEDSRYMKPGKELKVLSYPAHEQIALLVP
EKLTPHLKYYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFEPTQ
ARMAFPCFDEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLEDHF
ETTVKMSTYLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYALQAS
LKLLDFYEKYFDIYYPLSKLDLIAIPDFAPGAMENWGLITYRETSLLFDP
KTSSASDKLWVTRVIAHELAHQWFGNLVTMEWWNDIWLNEGFAKYMELIA
VNATYPELQFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMFDEV
SYNKGACILNMLKDFLGEEKFQKGIIQYLKKFSYRNAKNDDLWSSLSNVK
EMMTTWTLQKGIPLLVVKQDGCSLRLQQERFLQGVFQEDPEWRALQERYL
WHIPLTYSTNVIHRHILKSKTDTLDTSWVKFNVDSNGYYIVHYEGHGWDQ
LITQLNQNHTLLRPKDRVGLIHDVFQLVGAGRLTLDKALDMTYYLQHETS
SPALLEGLSYLESFYHMMDRRNISDISENLKRYLLQYFKPVIDRQSWSDK
GSVWDRMLRSALLKLACDLNHAPCIQKAAELFSQWMESSGKLNIPTDVLK
IVYSVGAQTTAGWNYLLEQYELSMSSAEQNKILYALSTSKHQEKLLKLIE
LGMEGKVIKTQNLAALLHAIARRPKGQQLAWDFVRENWTHLLKKFDLGSY
DIRMIISGTTAHFSSKDKLQEVKLFFESLEAQGSHLDIFQTVLETITKNI
KWLEKNLPTLRTWLMVNTR
3D structure
PDB6ea4 Crystal structure of human ER aminopeptidase 1 bound to aryl sulfonamide inhibitor.
ChainB
Resolution2.45 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) 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 ZN B H370 H374 E393 H317 H321 E340
BS02 J2G B G334 A335 R345 W363 R366 K397 E400 G281 A282 R292 W310 R313 K344 E347
BS03 LYS B E200 P333 A335 M336 E337 E393 Y455 E147 P280 A282 M283 E284 E340 Y402
BS04 LYS B T347 W363 N822 T294 W310 N730
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:6ea4, PDBe:6ea4, PDBj:6ea4
PDBsum6ea4
PubMed
UniProtQ6P179|ERAP2_HUMAN Endoplasmic reticulum aminopeptidase 2 (Gene Name=ERAP2)

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