Structure of PDB 6ea4 Chain A Binding Site BS02

Receptor Information
>6ea4 Chain A (length=883) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
FPVATNGERFPWQELRLPSVVIPLHYDLFVHPNLTSLDFVASEKIEVLVS
NATQFIILHSKDLEITNATLQSEEDSRYMKPGKELKVLSYPAHEQIALLV
PEKLTPHLKYYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFEPT
QARMAFPCFDEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLEDH
FETTVKMSTYLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYALQA
SLKLLDFYEKYFDIYYPLSKLDLIAIPDFAPGAMENWGLITYRETSLLFD
PKTSSASDKLWVTRVIAHELAHQWFGNLVTMEWWNDIWLNEGFAKYMELI
AVNATYPELQFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMFDE
VSYNKGACILNMLKDFLGEEKFQKGIIQYLKKFSYRNAKNDDLWSSLSNE
NAEVKEMMTTWTLQKGIPLLVVKQDGCSLRLQQERFLQGVFQEDPEWRAL
QERYLWHIPLTYSTSSSNVIHRHILKSKTDTLDLPEKTSWVKFNVDSNGY
YIVHYEGHGWDQLITQLNQNHTLLRPKDRVGLIHDVFQLVGAGRLTLDKA
LDMTYYLQHETSSPALLEGLSYLESFYHMMDRRNISDISENLKRYLLQYF
KPVIDRQSWSDKGSVWDRMLRSALLKLACDLNHAPCIQKAAELFSQWMES
SGKLNIPTDVLKIVYSVGAQTTAGWNYLLEQYELSMSSAEQNKILYALST
SKHQEKLLKLIELGMEGKVIKTQNLAALLHAIARRPKGQQLAWDFVRENW
THLLKKFDLGSYDIRMIISGTTAHFSSKDKLQEVKLFFESLEAQGSHLDI
FQTVLETITKNIKWLEKNLPTLRTWLMVNTRHH
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain6ea4 Chain A Residue 1001 [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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PDB6ea4 Crystal structure of human ER aminopeptidase 1 bound to aryl sulfonamide inhibitor.
Resolution2.45 Å
Binding residue
(original residue number in PDB)		H370 H374 E393
Binding residue
(residue number reindexed from 1)		H318 H322 E341
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) E337 H370 E371 H374 E393 Q447 Y455
Catalytic site (residue number reindexed from 1) E285 H318 E319 H322 E341 Q395 Y403
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:6ea4, PDBe:6ea4, PDBj:6ea4
PDBsum6ea4
PubMed
UniProtQ6P179|ERAP2_HUMAN Endoplasmic reticulum aminopeptidase 2 (Gene Name=ERAP2)

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