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1ASQ

X-RAY STRUCTURES AND MECHANISTIC IMPLICATIONS OF THREE FUNCTIONAL DERIVATIVES OF ASCORBATE OXIDASE FROM ZUCCHINI: REDUCED-, PEROXIDE-, AND AZIDE-FORMS

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0005576cellular_componentextracellular region
A0008447molecular_functionL-ascorbate oxidase activity
A0009506cellular_componentplasmodesma
A0009615biological_processresponse to virus
A0016491molecular_functionoxidoreductase activity
A0042542biological_processresponse to hydrogen peroxide
A0046872molecular_functionmetal ion binding
A0050687biological_processnegative regulation of defense response to virus
B0005507molecular_functioncopper ion binding
B0005576cellular_componentextracellular region
B0008447molecular_functionL-ascorbate oxidase activity
B0009506cellular_componentplasmodesma
B0009615biological_processresponse to virus
B0016491molecular_functionoxidoreductase activity
B0042542biological_processresponse to hydrogen peroxide
B0046872molecular_functionmetal ion binding
B0050687biological_processnegative regulation of defense response to virus
Functional Information from PROSITE/UniProt
site_idPS00079
Number of Residues21
DetailsMULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GvWaFhChIEphLhMGMgvvF
ChainResidueDetails
AGLY501-PHE521

site_idPS00080
Number of Residues12
DetailsMULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHiepHlhmGM
ChainResidueDetails
AHIS506-MET517

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues242
DetailsDomain: {"description":"Plastocyanin-like 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues332
DetailsDomain: {"description":"Plastocyanin-like 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues358
DetailsDomain: {"description":"Plastocyanin-like 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"description":"type 2 copper site","evidences":[{"source":"PubMed","id":"1548698","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues12
DetailsBinding site: {"description":"type 3 copper site","evidences":[{"source":"PubMed","id":"1548698","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsBinding site: {"description":"type 1 copper site","evidences":[{"source":"PubMed","id":"1548698","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000149","evidences":[{"source":"PubMed","id":"1548698","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a65
ChainResidueDetails
AHIS506
ACYS507
AHIS508

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a65
ChainResidueDetails
BHIS506
BCYS507
BHIS508

238895

PDB entries from 2025-07-16

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