Structure of PDB 3qnf Chain C

Receptor sequence
>3qnfC (length=800) Species: 9606 (Homo sapiens) [Search protein sequence]
FPWNKIRLPEYVIPVHYDLLIHANLTTLTFWGTTKVEITASQPTSTIILH
SHHLQISRATLRKGALSEEPLQVLEHPRQEQIALLAPEPLLVGLPYTVVI
HYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAF
KASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTVKMSTYLVAF
IISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSI
PYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITM
TVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPELKVGDY
FFGKCFDAMEVDALNSSHPVSTPVENPDVSYDKGACILNMLREYLSADAF
KSGIVQYLQKHSYKNTKNEDLWDSMASIVDVKTMMNTWTLQKGFPLITIT
VRGRNVHMKQEHYMKTGYLWHVPLTFITSKSDMVHRFLLKTKTDVLILPE
EVEWIKFNVGMNGYYIVHYEDDGWDSLTGLLKGTHTAVSSNDRASLINNA
FQLVSIGKLSIEKALDLSLYLKHETEIMPVFQGLNELIPMYKLMEKRDMN
EVETQFKAFLIRLLRDLIDKQTWTDEGSVSERMLRSQLLLLACVHNYQPC
VQRAEGYFRKWKESNGNLSLPVDVTLAVFAVGAQSTEGWDFLYSKYQFSL
SSTEKSQIEFALCRTQNKEKLQWLLQILTLIGRNPVGYPLAWQFLRKSIA
HMVMGTTNQFSTRTRLEEVKGQQTIETIEENIGWMDKNFDKIRVWLQSEK
3D structure
PDB3qnf Crystal structures of the endoplasmic reticulum aminopeptidase-1 (ERAP1) reveal the molecular basis for N-terminal peptide trimming.
ChainC
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E320 H353 E354 H357 E376 Y438
Catalytic site (residue number reindexed from 1) E271 H304 E305 H308 E327 Y381
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 C H353 H357 E376 H304 H308 E327
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:3qnf, PDBe:3qnf, PDBj:3qnf
PDBsum3qnf
PubMed21508329
UniProtQ9NZ08|ERAP1_HUMAN Endoplasmic reticulum aminopeptidase 1 (Gene Name=ERAP1)

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