Structure of PDB 3mdj Chain C

Receptor sequence
>3mdjC (length=819) Species: 9606 (Homo sapiens) [Search protein sequence]
PFPWNKIRLPEYVIPVHYDLLIHANLTTLTFWGTTKVEITASQPTSTIIL
HSHHLQISRATLRKGERLSEEPLQVLEHPRQEQIALLAPEPLLVGLPYTV
VIHYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEP
AFKASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTVKMSTYLV
AFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYF
SIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLDI
TMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPELKVG
DYFFGKCFDAMEVDALNSSDDVSYDKGACILNMLREYLSADAFKSGIVQY
LQKHSYKNTKNEDLWDSMASIVDVKTMMNTWTLQRGFPLITITVRGRNVH
MKQEHYMKAPDTGYLWHVPLTFITSKSDMVHRFLLKTKTDVLILPEEVEW
IKFNVGMNGYYIVHYEDDGWDSLTGLLKGTHTAVSSNDRASLINNAFQLV
SIGKLSIEKALDLSLYLKHETEIMPVFQGLNELIPMYKLMEKRDMNEVET
QFKAFLIRLLRDLIDKQTWTDEGSVSERMLRSELLLLACVHNYQPCVQRA
EGYFRKWKESNGNLSLPVDVTLAVFAVGAQSTEGWDFLYSKYQFSLSSTE
KSQIEFALCRTQNKEKLQWLLDESFKGDKIKTQEFPQILTLIGRNPVGYP
LAWQFLRKNWNKLVQKSSSIAHMVMGTTNQFSTRTRLEEVKCVQQTIETI
EENIGWMDKNFDKIRVWLQ
3D structure
PDB3mdj Structural basis for antigenic peptide precursor processing by the endoplasmic reticulum aminopeptidase ERAP1.
ChainC
Resolution2.95 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) E273 H306 E307 H310 E329 Y374
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 H306 H310 E329
BS02 BES C E183 G317 A318 M319 E320 T350 E354 E136 G270 A271 M272 E273 T303 E307 BindingDB: IC50=50000nM
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:3mdj, PDBe:3mdj, PDBj:3mdj
PDBsum3mdj
PubMed21478864
UniProtQ9NZ08|ERAP1_HUMAN Endoplasmic reticulum aminopeptidase 1 (Gene Name=ERAP1)

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