Structure of PDB 6m8p Chain R

Receptor sequence
>6m8pR (length=861) Species: 9606 (Homo sapiens) [Search protein sequence]
PFPWNKIRLPEYVIPVHYDLLIHANLTTLTFWGTTKVEITASQPTSTIIL
HSHHLQISRATLRKGLSEEPLQVLEHPRQEQIALLAPEPLLVGLPYTVVI
HYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAF
KASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTVKMSTYLVAF
IISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSI
PYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITM
TVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPELKVGDY
FFGKCFDAMEVDALNSSHPVSTPVENPAQIREMFDDVSYDKGACILNMLR
EYLSADAFKSGIVQYLQKHSYKNTKNEDLWDSMASIGGGGVDVKTMMNTW
TLQKGFPLITITVRGRNVHMKQEHYMKGDTGYLWHVPLTFITSKSDMVHR
FLLKTKTDVLILPEEVEWIKFNVGMNGYYIVHYEDDGWDSLTGLLKGTHT
AVSSNDRASLINNAFQLVSIGKLSIEKALDLSLYLKHETEIMPVFQGLNE
LIPMYKLMEKRDMNEVETQFKAFLIRLLRDLIDKQTWTDEGSVSERMLRS
QLLLLACVHNYQPCVQRAEGYFRKWKESNGNLSLPVDVTLAVFAVGAQST
EGWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKLQWLLDESFKGDKIKT
QEFPQILTLIGRNPVGYPLAWQFLRKNWNKLVQKFELGSSSIAHMVMGTT
NQFSTRTRLEEVKGFFSSLKENGSQLRCVQQTIETIEENIGWMDKNFDKI
RVWLQSEKLER
3D structure
PDB6m8p Conformational dynamics linked to domain closure and substrate binding explain the ERAP1 allosteric regulation mechanism.
ChainR
Resolution3.31 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) E271 H304 E305 H308 E327 R381 Y389
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 R H353 H357 E376 H304 H308 E327
BS02 P52 R E183 S316 G317 A318 E320 H353 E354 E376 F433 Y438 S844 E134 S267 G268 A269 E271 H304 E305 E327 F384 Y389 S790 BindingDB: IC50=33nM
Gene Ontology
Molecular Function
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6m8p, PDBe:6m8p, PDBj:6m8p
PDBsum6m8p
PubMed34489420
UniProtQ9NZ08|ERAP1_HUMAN Endoplasmic reticulum aminopeptidase 1 (Gene Name=ERAP1)

[Back to BioLiP]