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3SE6

Crystal structure of the human Endoplasmic Reticulum Aminopeptidase 2

Functional Information from GO Data
ChainGOidnamespacecontents
A0002250biological_processadaptive immune response
A0002474biological_processantigen processing and presentation of peptide antigen via MHC class I
A0004175molecular_functionendopeptidase activity
A0004177molecular_functionaminopeptidase activity
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0005789cellular_componentendoplasmic reticulum membrane
A0006508biological_processproteolysis
A0008217biological_processregulation of blood pressure
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0016020cellular_componentmembrane
A0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
A0042277molecular_functionpeptide binding
A0043171biological_processpeptide catabolic process
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
B0002250biological_processadaptive immune response
B0002474biological_processantigen processing and presentation of peptide antigen via MHC class I
B0004175molecular_functionendopeptidase activity
B0004177molecular_functionaminopeptidase activity
B0005515molecular_functionprotein binding
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005788cellular_componentendoplasmic reticulum lumen
B0005789cellular_componentendoplasmic reticulum membrane
B0006508biological_processproteolysis
B0008217biological_processregulation of blood pressure
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0016020cellular_componentmembrane
B0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
B0042277molecular_functionpeptide binding
B0043171biological_processpeptide catabolic process
B0046872molecular_functionmetal ion binding
B0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIAHELAHQW
ChainResidueDetails
AVAL367-TRP376

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues38
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AMET1-ARG20
BMET1-ARG20

site_idSWS_FT_FI2
Number of Residues38
DetailsTRANSMEM: Helical; Signal-anchor for type II membrane protein => ECO:0000255
ChainResidueDetails
AGLY21-VAL40
BGLY21-VAL40

site_idSWS_FT_FI3
Number of Residues1838
DetailsTOPO_DOM: Lumenal => ECO:0000255
ChainResidueDetails
APRO41-THR960
BPRO41-THR960

site_idSWS_FT_FI4
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:22106953
ChainResidueDetails
AGLU371
BGLU371

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22106953
ChainResidueDetails
AGLU200
BGLU200

site_idSWS_FT_FI6
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AGLY334
AHIS370
AHIS374
AGLU393
BGLY334
BHIS370
BHIS374
BGLU393

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Transition state stabilizer
ChainResidueDetails
ATYR455
BTYR455

site_idSWS_FT_FI8
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22106953
ChainResidueDetails
AASN85
AASN219
AASN405
AASN650
BASN85
BASN219
BASN405
BASN650

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
AASN119
BASN119

227561

PDB entries from 2024-11-20

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