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5LHD

Structure of glycosylated human aminopeptidase N

Functional Information from GO Data
ChainGOidnamespacecontents
A0001525biological_processangiogenesis
A0001618molecular_functionvirus receptor activity
A0004177molecular_functionaminopeptidase activity
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
A0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0009897cellular_componentexternal side of plasma membrane
A0030154biological_processcell differentiation
A0030667cellular_componentsecretory granule membrane
A0038023molecular_functionsignaling receptor activity
A0042277molecular_functionpeptide binding
A0043171biological_processpeptide catabolic process
A0046718biological_processsymbiont entry into host cell
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
A0070062cellular_componentextracellular exosome
B0001525biological_processangiogenesis
B0001618molecular_functionvirus receptor activity
B0004177molecular_functionaminopeptidase activity
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005765cellular_componentlysosomal membrane
B0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
B0005886cellular_componentplasma membrane
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0009897cellular_componentexternal side of plasma membrane
B0030154biological_processcell differentiation
B0030667cellular_componentsecretory granule membrane
B0038023molecular_functionsignaling receptor activity
B0042277molecular_functionpeptide binding
B0043171biological_processpeptide catabolic process
B0046718biological_processsymbiont entry into host cell
B0046872molecular_functionmetal ion binding
B0070006molecular_functionmetalloaminopeptidase activity
B0070062cellular_componentextracellular exosome
C0001525biological_processangiogenesis
C0001618molecular_functionvirus receptor activity
C0004177molecular_functionaminopeptidase activity
C0005615cellular_componentextracellular space
C0005737cellular_componentcytoplasm
C0005765cellular_componentlysosomal membrane
C0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
C0005886cellular_componentplasma membrane
C0006508biological_processproteolysis
C0008237molecular_functionmetallopeptidase activity
C0008270molecular_functionzinc ion binding
C0009897cellular_componentexternal side of plasma membrane
C0030154biological_processcell differentiation
C0030667cellular_componentsecretory granule membrane
C0038023molecular_functionsignaling receptor activity
C0042277molecular_functionpeptide binding
C0043171biological_processpeptide catabolic process
C0046718biological_processsymbiont entry into host cell
C0046872molecular_functionmetal ion binding
C0070006molecular_functionmetalloaminopeptidase activity
C0070062cellular_componentextracellular exosome
D0001525biological_processangiogenesis
D0001618molecular_functionvirus receptor activity
D0004177molecular_functionaminopeptidase activity
D0005615cellular_componentextracellular space
D0005737cellular_componentcytoplasm
D0005765cellular_componentlysosomal membrane
D0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
D0005886cellular_componentplasma membrane
D0006508biological_processproteolysis
D0008237molecular_functionmetallopeptidase activity
D0008270molecular_functionzinc ion binding
D0009897cellular_componentexternal side of plasma membrane
D0030154biological_processcell differentiation
D0030667cellular_componentsecretory granule membrane
D0038023molecular_functionsignaling receptor activity
D0042277molecular_functionpeptide binding
D0043171biological_processpeptide catabolic process
D0046718biological_processsymbiont entry into host cell
D0046872molecular_functionmetal ion binding
D0070006molecular_functionmetalloaminopeptidase activity
D0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIAHELAHQW
ChainResidueDetails
AVAL385-TRP394

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:22932899
ChainResidueDetails
AGLU389
BGLU389
CGLU389
DGLU389

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22932899
ChainResidueDetails
AGLY352
BGLY352
CGLY352
DGLY352

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:22932899, ECO:0007744|PDB:4FYQ, ECO:0007744|PDB:4FYR, ECO:0007744|PDB:4FYT
ChainResidueDetails
AHIS388
DHIS388
DHIS392
DGLU411
AHIS392
AGLU411
BHIS388
BHIS392
BGLU411
CHIS388
CHIS392
CGLU411

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Transition state stabilizer => ECO:0000269|PubMed:22932899
ChainResidueDetails
ATYR477
BTYR477
CTYR477
DTYR477

site_idSWS_FT_FI5
Number of Residues16
DetailsMOD_RES: Sulfotyrosine => ECO:0000255
ChainResidueDetails
ATYR176
CTYR419
CTYR424
CTYR913
DTYR176
DTYR419
DTYR424
DTYR913
ATYR419
ATYR424
ATYR913
BTYR176
BTYR419
BTYR424
BTYR913
CTYR176

site_idSWS_FT_FI6
Number of Residues16
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899
ChainResidueDetails
AASN128
CASN234
CASN681
CASN818
DASN128
DASN234
DASN681
DASN818
AASN234
AASN681
AASN818
BASN128
BASN234
BASN681
BASN818
CASN128

site_idSWS_FT_FI7
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899
ChainResidueDetails
AASN265
BASN265
CASN265
DASN265

site_idSWS_FT_FI8
Number of Residues12
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22932899
ChainResidueDetails
AASN319
DASN319
DASN527
DASN625
AASN527
AASN625
BASN319
BASN527
BASN625
CASN319
CASN527
CASN625

site_idSWS_FT_FI9
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN573
BASN573
CASN573
DASN573

site_idSWS_FT_FI10
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AASN735
BASN735
CASN735
DASN735

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PDB entries from 2024-07-24

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