Structure of PDB 6mgq Chain C

Receptor sequence
>6mgqC (length=843) Species: 9606 (Homo sapiens) [Search protein sequence]
SDGTPFPWNKIRLPEYVIPVHYDLLIHANLTTLTFWGTTKVEITASQPTS
TIILHSHHLQISRATLRKGAGERLSEEPLQVLEHPRQEQIALLAPEPLLV
GLPYTVVIHYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAF
PCFDEPAFKASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTVK
MSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLE
FYEDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSA
SSKLDITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTH
PELKVGDYFFGKCFDAMEVDALNSSHPVSTPVENPAQIREMFDDVSYDKG
ACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWDSMASICPTDER
VDVKTMMNTWTLQRGFPLITITVRGRNVHMKQEHYMKGSDGAPDTGYLWH
VPLTFITSKSDMVHRFLLKTKTDVLILPEEVEWIKFNVGMNGYYIVHYED
DGWDSLTGLLKGTHTAVSSNDRASLINNAFQLVSIGKLSIEKALDLSLYL
KHETEIMPVFQGLNELIPMYKLMEKRDMNEVETQFKAFLIRLLRDLIDKQ
TWTDEGSVSERMLRSELLLLACVHNYQPCVQRAEGYFRKWKESNGNLSLP
VDVTLAVFAVGAQSTEGWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKL
QWLLDESFIKTQEFPQILTLIGRNPVGYPLAWQFLRKNWNKLVQKFELVM
GTTNQFSTRTRLEEVQQTIETIEENIGWMDKNFDKIRVWLQSE
3D structure
PDB6mgq Conformational dynamics linked to domain closure and substrate binding explain the ERAP1 allosteric regulation mechanism.
ChainC
Resolution2.92 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) E320 H353 E354 H357 E376 R430 Y438
Catalytic site (residue number reindexed from 1) E279 H312 E313 H316 E335 R389 Y397
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 peptide C E183 S316 A318 D346 T350 H353 E354 E376 K380 E383 Y399 K403 R430 D435 E142 S275 A277 D305 T309 H312 E313 E335 K339 E342 Y358 K362 R389 D394
BS02 ZN C H353 H357 E376 H312 H316 E335
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

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

[Back to BioLiP]