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3K5T

Crystal structure of human diamine oxidase in space group C2221

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 amine oxidase activity
A0008201molecular_functionheparin binding
A0009308biological_processamine metabolic process
A0009445biological_processputrescine metabolic process
A0016491molecular_functionoxidoreductase activity
A0035580cellular_componentspecific granule lumen
A0042803molecular_functionprotein homodimerization activity
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
A0048038molecular_functionquinone binding
A0050232molecular_functionputrescine oxidase activity
A0052597molecular_functiondiamine oxidase activity
A0052598molecular_functionhistamine oxidase activity
A0052599molecular_functionmethylputrescine oxidase activity
A0052600molecular_functionpropane-1,3-diamine oxidase activity
A0070062cellular_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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:19764817
ChainResidueDetails
AASP373

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Schiff-base intermediate with substrate; via topaquinone => ECO:0000269|PubMed:19764817, ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T
ChainResidueDetails
ATPQ461

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:19764817, ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T, ECO:0007744|PDB:3MPH
ChainResidueDetails
AASP519
ALEU520
AASP521
AGLU562
APHE653
AASN656
AGLU658
AASP664
ALEU665
AHIS675
AHIS510
AHIS512

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: 2',4',5'-topaquinone => ECO:0000269|PubMed:19764817
ChainResidueDetails
ATPQ461

site_idSWS_FT_FI5
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19764817, ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T, ECO:0007744|PDB:3MPH
ChainResidueDetails
AASN538
AASN745
AASN110

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN168

220472

PDB entries from 2024-05-29

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