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1ASP

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
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
B0005507molecular_functioncopper ion binding
B0005576cellular_componentextracellular region
B0008447molecular_functionL-ascorbate oxidase activity
B0009506cellular_componentplasmodesma
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
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 Residues4
DetailsBINDING: type 2 copper site => ECO:0000269|PubMed:1548698
ChainResidueDetails
AHIS60
AHIS448
BHIS60
BHIS448

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: type 3 copper site => ECO:0000269|PubMed:1548698
ChainResidueDetails
AHIS62
BHIS450
BHIS506
BHIS508
AHIS104
AHIS106
AHIS450
AHIS506
AHIS508
BHIS62
BHIS104
BHIS106

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: type 1 copper site => ECO:0000269|PubMed:1548698
ChainResidueDetails
AHIS445
ACYS507
AHIS512
AMET517
BHIS445
BCYS507
BHIS512
BMET517

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:1548698
ChainResidueDetails
AASN92
BASN92

site_idSWS_FT_FI5
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN325
AASN440
BASN325
BASN440

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

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PDB entries from 2024-10-30

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