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2Y9X

Crystal structure of PPO3, a tyrosinase from Agaricus bisporus, in deoxy-form that contains additional unknown lectin-like subunit, with inhibitor tropolone

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
B0016491molecular_functionoxidoreductase activity
C0016491molecular_functionoxidoreductase activity
D0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 400
ChainResidue
AHIS61
ACYS83
AHIS85
AHIS94

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 401
ChainResidue
AHIS259
AHIS263
AHIS296
A0TR410

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 0TR A 410
ChainResidue
AHIS263
APHE264
AMET280
AVAL283
AALA286
ACU401
AASN260

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HO A 402
ChainResidue
AASP336
AGLN351
AASP353
BASP312

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 400
ChainResidue
BHIS61
BCYS83
BHIS85
BHIS94

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 401
ChainResidue
BHIS259
BHIS263
BHIS296
B0TR410

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HO B 402
ChainResidue
AASP312
BASP336
BGLN351
BASP353

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 0TR B 410
ChainResidue
BASN260
BHIS263
BPHE264
BVAL283
BALA286
BCU401

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU C 400
ChainResidue
CHIS61
CCYS83
CHIS85
CHIS94
C0TR410

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 401
ChainResidue
CHIS259
CHIS263
CHIS296
C0TR410

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HO C 402
ChainResidue
CASP336
CGLN351
CASP353
CHOH2002
DASP312

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 0TR C 410
ChainResidue
CHIS61
CHIS85
CHIS259
CASN260
CHIS263
CVAL283
CALA286
CCU400
CCU401

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU D 400
ChainResidue
DHIS61
DCYS83
DHIS85
DHIS94
D0TR410

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU D 401
ChainResidue
DHIS259
DHIS263
DHIS296
D0TR410

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HO D 402
ChainResidue
CASP312
DASP336
DGLN351
DASP353
DHOH2003

site_idBC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 0TR D 410
ChainResidue
DHIS61
DHIS85
DHIS259
DASN260
DHIS263
DMET280
DVAL283
DALA286
DPHE292
DCU400
DCU401

Functional Information from PROSITE/UniProt
site_idPS00498
Number of Residues12
DetailsTYROSINASE_2 Tyrosinase and hemocyanins CuB-binding region signature. DPiFWmhHcnvD
ChainResidueDetails
AASP289-ASP300

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:21598903
ChainResidueDetails
AHIS61
BHIS259
BHIS263
BHIS296
CHIS61
CHIS85
CHIS94
CHIS259
CHIS263
CHIS296
DHIS61
AHIS85
DHIS85
DHIS94
DHIS259
DHIS263
DHIS296
AHIS94
AHIS259
AHIS263
AHIS296
BHIS61
BHIS85
BHIS94

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Cleavage => ECO:0000305
ChainResidueDetails
AGLY392
BGLY392
CGLY392
DGLY392

site_idSWS_FT_FI3
Number of Residues8
DetailsCROSSLNK: 2'-(S-cysteinyl)-histidine (Cys-His) => ECO:0000269|PubMed:21598903
ChainResidueDetails
ACYS83
AHIS85
BCYS83
BHIS85
CCYS83
CHIS85
DCYS83
DHIS85

222624

PDB entries from 2024-07-17

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