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3HII

Crystal structure of human diamine oxidase in complex with the inhibitor pentamidine

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005777cellular_componentperoxisome
A0005886cellular_componentplasma membrane
A0005923cellular_componentbicellular tight junction
A0008131molecular_functionprimary methylamine oxidase activity
A0008201molecular_functionheparin binding
A0009308biological_processamine metabolic process
A0009445biological_processputrescine metabolic process
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0035580cellular_componentspecific granule lumen
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0048038molecular_functionquinone binding
A0050232molecular_functionputrescine oxidase activity
A0052597molecular_functiondiamine oxidase activity
A0052598molecular_functionhistamine oxidase activity
A0070062cellular_componentextracellular exosome
B0005507molecular_functioncopper ion binding
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005777cellular_componentperoxisome
B0005886cellular_componentplasma membrane
B0005923cellular_componentbicellular tight junction
B0008131molecular_functionprimary methylamine oxidase activity
B0008201molecular_functionheparin binding
B0009308biological_processamine metabolic process
B0009445biological_processputrescine metabolic process
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0035580cellular_componentspecific granule lumen
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0048038molecular_functionquinone binding
B0050232molecular_functionputrescine oxidase activity
B0052597molecular_functiondiamine oxidase activity
B0052598molecular_functionhistamine oxidase activity
B0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS01164
Number of Residues14
DetailsCOPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LVLrttsTvyNYDY
ChainResidueDetails
ALEU450-TYR463

site_idPS01165
Number of Residues14
DetailsCOPPER_AMINE_OXID_2 Copper amine oxidase copper-binding site signature. TvGflHIphsEDiP
ChainResidueDetails
ATHR670-PRO683

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"19764817","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Schiff-base intermediate with substrate; via topaquinone","evidences":[{"source":"PubMed","id":"19764817","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HI7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HIG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HII","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3K5T","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19764817","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HI7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HIG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HII","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3K5T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MPH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"2',4',5'-topaquinone","evidences":[{"source":"PubMed","id":"19764817","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19764817","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HI7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HIG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HII","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3K5T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MPH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oac
ChainResidueDetails
AASP373

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oac
ChainResidueDetails
BASP373

239803

PDB entries from 2025-08-06

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