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6XIZ

Crystal structure of multi-copper oxidase from Pediococcus acidilactici

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0016491molecular_functionoxidoreductase activity
B0005507molecular_functioncopper ion binding
B0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CU A 501
ChainResidue
AHIS389
ACYS443
AHIS448
AMET453

site_idAC2
Number of Residues10
Detailsbinding site for residue C2O A 502
ChainResidue
AHIS394
AHIS442
AHIS444
ACU503
AHOH610
AHIS104
AHIS106
AHIS145
AHIS147
AHIS392

site_idAC3
Number of Residues6
Detailsbinding site for residue CU A 503
ChainResidue
AHIS104
AHIS106
AHIS392
AHIS394
AC2O502
AHOH788

site_idAC4
Number of Residues4
Detailsbinding site for residue CU B 501
ChainResidue
BHIS389
BCYS443
BHIS448
BMET453

site_idAC5
Number of Residues10
Detailsbinding site for residue C2O B 502
ChainResidue
BHIS104
BHIS106
BHIS145
BHIS147
BHIS392
BHIS394
BHIS442
BHIS444
BCU503
BHOH609

site_idAC6
Number of Residues6
Detailsbinding site for residue CU B 503
ChainResidue
BHIS104
BHIS106
BHIS392
BHIS394
BC2O502
BHOH783

site_idAC7
Number of Residues7
Detailsbinding site for residue BEN B 504
ChainResidue
ATYR14
AHOH715
AHOH757
BTYR14
BASP303
BHOH693
BHOH704

site_idAC8
Number of Residues1
Detailsbinding site for residue CL B 505
ChainResidue
BPRO223

Functional Information from PROSITE/UniProt
site_idPS00079
Number of Residues21
DetailsMULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GiFmYhChILehEdTGMmaqI
ChainResidueDetails
AGLY437-ILE457

site_idPS00080
Number of Residues12
DetailsMULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHileHedtGM
ChainResidueDetails
AHIS442-MET453

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PDB entries from 2024-10-09

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