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2XLL

The crystal structure of bilirubin oxidase from Myrothecium verrucaria

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
A0047705molecular_functionbilirubin oxidase activity
B0005507molecular_functioncopper ion binding
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
B0047705molecular_functionbilirubin oxidase activity
C0005507molecular_functioncopper ion binding
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
C0047705molecular_functionbilirubin oxidase activity
D0005507molecular_functioncopper ion binding
D0016491molecular_functionoxidoreductase activity
D0046872molecular_functionmetal ion binding
D0047705molecular_functionbilirubin oxidase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: type 2 copper site => ECO:0000250
ChainResidueDetails
AHIS94
AHIS401
BHIS94
BHIS401
CHIS94
CHIS401
DHIS94
DHIS401

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: type 3 copper site => ECO:0000250
ChainResidueDetails
AHIS96
BHIS403
BHIS456
BHIS458
CHIS96
CHIS134
CHIS136
CHIS403
CHIS456
CHIS458
DHIS96
AHIS134
DHIS134
DHIS136
DHIS403
DHIS456
DHIS458
AHIS136
AHIS403
AHIS456
AHIS458
BHIS96
BHIS134
BHIS136

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: type 1 copper site => ECO:0000250
ChainResidueDetails
AHIS398
CCYS457
CHIS462
CMET467
DHIS398
DCYS457
DHIS462
DMET467
ACYS457
AHIS462
AMET467
BHIS398
BCYS457
BHIS462
BMET467
CHIS398

site_idSWS_FT_FI4
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN472
AASN482
BASN472
BASN482
CASN472
CASN482
DASN472
DASN482

218853

PDB entries from 2024-04-24

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