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2Y73

THE NATIVE STRUCTURES OF SOLUBLE HUMAN PRIMARY AMINE OXIDASE AOC3

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005769cellular_componentearly endosome
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0005886cellular_componentplasma membrane
A0005902cellular_componentmicrovillus
A0006954biological_processinflammatory response
A0007155biological_processcell adhesion
A0008131molecular_functionprimary methylamine oxidase activity
A0009308biological_processamine metabolic process
A0009986cellular_componentcell surface
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016641molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0046982molecular_functionprotein heterodimerization activity
A0048038molecular_functionquinone binding
A0052595molecular_functionaliphatic amine oxidase activity
B0005507molecular_functioncopper ion binding
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005769cellular_componentearly endosome
B0005783cellular_componentendoplasmic reticulum
B0005794cellular_componentGolgi apparatus
B0005886cellular_componentplasma membrane
B0005902cellular_componentmicrovillus
B0006954biological_processinflammatory response
B0007155biological_processcell adhesion
B0008131molecular_functionprimary methylamine oxidase activity
B0009308biological_processamine metabolic process
B0009986cellular_componentcell surface
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016641molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0046982molecular_functionprotein heterodimerization activity
B0048038molecular_functionquinone binding
B0052595molecular_functionaliphatic amine oxidase activity
Functional Information from PROSITE/UniProt
site_idPS01164
Number of Residues14
DetailsCOPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LVVrsmsTllNYDY
ChainResidueDetails
ALEU460-TYR473

site_idPS01165
Number of Residues14
DetailsCOPPER_AMINE_OXID_2 Copper amine oxidase copper-binding site signature. TaGflHIphaEDiP
ChainResidueDetails
ATHR679-PRO692

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:9653080
ChainResidueDetails
AMET1-THR5
BMET1-THR5

site_idSWS_FT_FI2
Number of Residues40
DetailsTRANSMEM: Helical; Signal-anchor for type II membrane protein => ECO:0000255
ChainResidueDetails
AILE6-VAL26
BILE6-VAL26

site_idSWS_FT_FI3
Number of Residues1472
DetailsTOPO_DOM: Extracellular => ECO:0000305|PubMed:9653080
ChainResidueDetails
AGLY27-ASN763
BGLY27-ASN763

site_idSWS_FT_FI4
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P19801
ChainResidueDetails
AASP386
BASP386

site_idSWS_FT_FI5
Number of Residues2
DetailsACT_SITE: Schiff-base intermediate with substrate; via topaquinone => ECO:0000269|PubMed:16046623, ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1
ChainResidueDetails
ATPQ471
BTPQ471

site_idSWS_FT_FI6
Number of Residues26
DetailsBINDING: BINDING => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1, ECO:0007744|PDB:4BTW, ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY
ChainResidueDetails
AHIS520
AGLU667
AASP673
ALEU674
AHIS684
BHIS520
BHIS522
BASP529
BLEU530
BASP531
BGLU572
AHIS522
BGLU641
BPHE663
BASN665
BGLU667
BASP673
BLEU674
BHIS684
AASP529
ALEU530
AASP531
AGLU572
AGLU641
APHE663
AASN665

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: 2',4',5'-topaquinone => ECO:0000269|PubMed:16046623, ECO:0007744|PDB:1PU4
ChainResidueDetails
ATPQ471
BTPQ471

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: O-linked (GalNAc...) serine => ECO:0000305|PubMed:16046623
ChainResidueDetails
ASER43
BSER43

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:19159218, ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1
ChainResidueDetails
AASN137
BASN137

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: O-linked (GalNAc...) threonine => ECO:0000305|PubMed:16046623
ChainResidueDetails
ATHR212
BTHR212

site_idSWS_FT_FI11
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1, ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY
ChainResidueDetails
AASN232
BASN232

site_idSWS_FT_FI12
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:4BTY
ChainResidueDetails
AASN294
BASN294

site_idSWS_FT_FI13
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:4BTW, ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY
ChainResidueDetails
AASN592
BASN592

site_idSWS_FT_FI14
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:4BTW, ECO:0007744|PDB:4BTX
ChainResidueDetails
AASN618
BASN618

site_idSWS_FT_FI15
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:4BTW, ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY
ChainResidueDetails
AASN666
BASN666

site_idSWS_FT_FI16
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) threonine => ECO:0000305|PubMed:16046623
ChainResidueDetails
ATHR679
BTHR679

227933

PDB entries from 2024-11-27

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