Structure of PDB 5j6s Chain B Binding Site BS02

Receptor Information
>5j6s Chain B (length=880) 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
KTSSASDKLWVTRVIAHELAHQWFGNLVTMEWWNDIWLNEGFAKYMELIA
VNATYPELQFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMFDEV
SYNKGACILNMLKDFLGEEKFQKGIIQYLKKFSYRNAKNDDLWSSLSNSE
VKEMMTTWTLQKGIPLLVVKQDGCSLRLQQERFLQGVFQEDPEWRALQER
YLWHIPLTYSTSSSNVIHRHILKSKTDTLDLPEKTSWVKFNVDSNGYYIV
HYEGHGWDQLITQLNQNHTLLRPKDRVGLIHDVFQLVGAGRLTLDKALDM
TYYLQHETSSPALLEGLSYLESFYHMMDRRNISDISENLKRYLLQYFKPV
IDRQSWSDKGSVWDRMLRSALLKLACDLNHAPCIQKAAELFSQWMESSGK
LNIPTDVLKIVYSVGAQTTAGWNYLLEQYELSMSSAEQNKILYALSTSKH
QEKLLKLIELGMEGKVIKTQNLAALLHAIARRPKGQQLAWDFVRENWTHL
LKKFDLGSYDIRMIISGTTAHFSSKDKLQEVKLFFESLEAQGSHLDIFQT
VLETITKNIKWLEKNLPTLRTWLMVNTRHH
Ligand information
Ligand ID6GA
InChIInChI=1S/C17H17FN2O3/c18-14-8-6-12(7-9-14)10-15(17(22)20-23)16(21)19-11-13-4-2-1-3-5-13/h1-9,15,23H,10-11H2,(H,19,21)(H,20,22)/t15-/m0/s1
InChIKeyUBULRDFJXZRBJH-HNNXBMFYSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=C(NCc1ccccc1)C(C(=O)NO)Cc2ccc(cc2)F
OpenEye OEToolkits 2.0.4c1ccc(cc1)CNC(=O)[C@H](Cc2ccc(cc2)F)C(=O)NO
CACTVS 3.385ONC(=O)[CH](Cc1ccc(F)cc1)C(=O)NCc2ccccc2
CACTVS 3.385ONC(=O)[C@@H](Cc1ccc(F)cc1)C(=O)NCc2ccccc2
OpenEye OEToolkits 2.0.4c1ccc(cc1)CNC(=O)C(Cc2ccc(cc2)F)C(=O)NO
FormulaC17 H17 F N2 O3
Name(2S)-N~1~-benzyl-2-[(4-fluorophenyl)methyl]-N~3~-hydroxypropanediamide
ChEMBL
DrugBank
ZINCZINC000095576973
PDB chain5j6s Chain B Residue 1015 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB5j6s Crystal Structures of ERAP2 Complexed with Inhibitors Reveal Pharmacophore Requirements for Optimizing Inhibitor Potency.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		E200 P333 A335 H370 E371 H374 E393 F450 Y455 Y892
Binding residue
(residue number reindexed from 1)		E147 P280 A282 H317 E318 H321 E340 F397 Y402 Y809
Annotation score1
Binding affinityBindingDB: IC50=>100000nM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5j6s, PDBe:5j6s, PDBj:5j6s
PDBsum5j6s
PubMed28337326
UniProtQ6P179|ERAP2_HUMAN Endoplasmic reticulum aminopeptidase 2 (Gene Name=ERAP2)

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