Structure of PDB 7sh0 Chain B

Receptor sequence
>7sh0B (length=841) Species: 9606 (Homo sapiens) [Search protein sequence]
PVATNGERFPWQELRLPSVVIPLHYDLFVHPNLTSLDFVASEKIEVLVSN
ATQFIILHSKDLEITNATLQYMKPGKELKVLSYPAHEQIALLVPEKLTPH
LKYYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFEPTQARMAFP
CFDEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLEDHFETTVKM
STYLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYALQASLKLLDF
YEKYFDIYYPLSKLDLIAIPDFAPGAMENWGLITYRETSLLFDPKTSSAS
DKLWVTRVIAHELAHQWFGNLVTMEWWNDIWLNEGFAKYMELIAVNATYP
ELQFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMFDEVSYNKGA
CILNMLKDFLGEEKFQKGIIQYLKKFSYRNAKNDDLWSSLFLGENAEVKE
MMTTWTLQKGIPLLQGVFQEDPEWRALQERYLWHIPLTYSTSSSNVIHRH
ILKSKTDTLDNVDSNGYYIVWDQLITQLNQNHTLLRPKDRVGLIHDVFQL
VGAGRLTLDKALDMTYYLQHETSSPALLEGLSYLESFYHMMDRRNISDIS
ENLKRYLLQYFKPVIDRQSWSDKGSVWDRMLRSALLKLACDLNHAPCIQK
AAELFSQWMESSGKLNIPTDVLKIVYSVGAQTTAGWNYLLEQYELSMSSA
EQNKILYALSTSKHQEKLLKLIELGMEGKVIKTQNLAALLHAIARRPKGQ
QLAWDFVRENWTHLLKKFDLGSYDIRMIISGTTAHFSSKDKLQEVKLFFE
SLEAQGSHLDIFQTVLETITKNIKWLEKNLPTLRTWLMVNT
3D structure
PDB7sh0 Discovery of the First Selective Nanomolar Inhibitors of ERAP2 by Kinetic Target-Guided Synthesis.
ChainB
Resolution3.2 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
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 H311 H315 E334
BS02 GIY B E200 P333 A335 E337 E371 H374 E393 F450 Y455 Y892 E141 P274 A276 E278 E312 H315 E334 F391 Y396 Y773
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:7sh0, PDBe:7sh0, PDBj:7sh0
PDBsum7sh0
PubMed35904863
UniProtQ6P179|ERAP2_HUMAN Endoplasmic reticulum aminopeptidase 2 (Gene Name=ERAP2)

[Back to BioLiP]