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1TU5

Crystal structure of bovine plasma copper-containing amine oxidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0005576cellular_componentextracellular region
A0005769cellular_componentearly endosome
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0005886cellular_componentplasma membrane
A0008131molecular_functionprimary amine oxidase activity
A0009308biological_processamine metabolic process
A0016491molecular_functionoxidoreductase activity
A0016641molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
A0048038molecular_functionquinone binding
A0052595molecular_functionaliphatic amine oxidase activity
B0005507molecular_functioncopper ion binding
B0005576cellular_componentextracellular region
B0005769cellular_componentearly endosome
B0005783cellular_componentendoplasmic reticulum
B0005794cellular_componentGolgi apparatus
B0005886cellular_componentplasma membrane
B0008131molecular_functionprimary amine oxidase activity
B0009308biological_processamine metabolic process
B0016491molecular_functionoxidoreductase activity
B0016641molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
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. LVFrsvsTmlNYDY
ChainResidueDetails
ALEU459-TYR472

site_idPS01165
Number of Residues14
DetailsCOPPER_AMINE_OXID_2 Copper amine oxidase copper-binding site signature. TaGflHIphaEDiP
ChainResidueDetails
ATHR678-PRO691

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P19801
ChainResidueDetails
AASP385
BASP385

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Schiff-base intermediate with substrate; via topaquinone => ECO:0007744|PDB:2PNC
ChainResidueDetails
ATPQ470
BTPQ470

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:2PNC
ChainResidueDetails
ATYR383
AMET467
BTYR383
BMET467

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15701511, ECO:0007744|PDB:1TU5, ECO:0007744|PDB:2PNC
ChainResidueDetails
AHIS519
AHIS521
AHIS683
BHIS519
BHIS521
BHIS683

site_idSWS_FT_FI5
Number of Residues18
DetailsBINDING: BINDING => ECO:0007744|PDB:1TU5, ECO:0007744|PDB:2PNC
ChainResidueDetails
AASP528
BASP528
BLEU529
BASP530
BGLU571
BPHE662
BASN664
BGLU666
BASP672
BLEU673
ALEU529
AASP530
AGLU571
APHE662
AASN664
AGLU666
AASP672
ALEU673

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: 2',4',5'-topaquinone => ECO:0007744|PDB:1TU5
ChainResidueDetails
ATPQ470
BTPQ470

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15701511, ECO:0007744|PDB:1TU5, ECO:0007744|PDB:2PNC
ChainResidueDetails
AASN136
BASN136

site_idSWS_FT_FI8
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15701511, ECO:0007744|PDB:1TU5
ChainResidueDetails
AASN231
AASN665
BASN231
BASN665

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oac
ChainResidueDetails
AASP385

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oac
ChainResidueDetails
BASP385

224004

PDB entries from 2024-08-21

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