Structure of PDB 6mgq Chain B Binding Site BS01

Receptor Information
>6mgq Chain B (length=858) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DGTPFPWNKIRLPEYVIPVHYDLLIHANLTTLTFWGTTKVEITASQPTST
IILHSHHLQISRATLRKGAGERLSEEPLQVLEHPRQEQIALLAPEPLLVG
LPYTVVIHYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAFP
CFDEPAFKASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTVKM
STYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEF
YEDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSAS
SKLDITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHP
ELKVGDYFFGKCFDAMEVDALNSSHPVSTPVENPAQIREMFDDVSYDKGA
CILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWDSMASIRVDVKTM
MNTWTLQRGFPLITITVRGRNVHMKQEHYMKGSDGAPDTGYLWHVPLTFI
TSKSDMVHRFLLKTKTDVLILPEEVEWIKFNVGMNGYYIVHYEDDGWDSL
TGLLKGTHTAVSSNDRASLINNAFQLVSIGKLSIEKALDLSLYLKHETEI
MPVFQGLNELIPMYKLMEKRDMNEVETQFKAFLIRLLRDLIDKQTWTDEG
SVSERMLRSELLLLACVHNYQPCVQRAEGYFRKWKESNGNLSLPVDVTLA
VFAVGAQSTEGWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKLQWLLDE
SFKGDILTLIGRNPVGYPLAWQFLRKNWNKLVQKFELGSSSIAHMVMGTT
NQFSTRTRLEEVKGFFSSLKENGSQLRCVQQTIETIEENIGWMDKNFDKI
RVWLQSEK
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6mgq Conformational dynamics linked to domain closure and substrate binding explain the ERAP1 allosteric regulation mechanism.
Resolution2.92 Å
Binding residue
(original residue number in PDB)		E183 S316 A318 E320 D346 T350 H353 E354 E376 K380 E383 Y399 K403 R430 D435
Binding residue
(residue number reindexed from 1)		E141 S274 A276 E278 D304 T308 H311 E312 E334 K338 E341 Y357 K361 R388 D393
Enzymatic activity
Catalytic site (original residue number in PDB) E320 H353 E354 H357 E376 R430 Y438
Catalytic site (residue number reindexed from 1) E278 H311 E312 H315 E334 R388 Y396
Enzyme Commision number 3.4.11.-
Gene Ontology
Molecular Function
GO:0004175 endopeptidase activity
GO:0004177 aminopeptidase activity
GO:0005138 interleukin-6 receptor binding
GO:0005151 interleukin-1, type II receptor binding
GO:0005515 protein binding
GO:0008233 peptidase activity
GO:0008235 metalloexopeptidase activity
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:0001525 angiogenesis
GO:0002250 adaptive immune response
GO:0002474 antigen processing and presentation of peptide antigen via MHC class I
GO:0006508 proteolysis
GO:0006509 membrane protein ectodomain proteolysis
GO:0008217 regulation of blood pressure
GO:0009617 response to bacterium
GO:0019885 antigen processing and presentation of endogenous peptide antigen via MHC class I
GO:0043171 peptide catabolic process
GO:0045088 regulation of innate immune response
GO:0045444 fat cell differentiation
GO:0045766 positive regulation of angiogenesis
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0005783 endoplasmic reticulum
GO:0005788 endoplasmic reticulum lumen
GO:0005789 endoplasmic reticulum membrane
GO:0005829 cytosol
GO:0016020 membrane
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6mgq, PDBe:6mgq, PDBj:6mgq
PDBsum6mgq
PubMed34489420
UniProtQ9NZ08|ERAP1_HUMAN Endoplasmic reticulum aminopeptidase 1 (Gene Name=ERAP1)

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