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6W2K

Crystal structure of laccase from Thermus thermophilus HB27 in reducing conditions (Na2,S2,O2, 20 min)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0016491molecular_functionoxidoreductase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0046872molecular_functionmetal ion binding
A0052716molecular_functionhydroquinone:oxygen oxidoreductase activity
B0005507molecular_functioncopper ion binding
B0016491molecular_functionoxidoreductase activity
B0030288cellular_componentouter membrane-bounded periplasmic space
B0046872molecular_functionmetal ion binding
B0052716molecular_functionhydroquinone:oxygen oxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MPD A 501
ChainResidue
APRO191
AMET295
AMET354
AMET355
ACU511

site_idAC2
Number of Residues5
Detailsbinding site for residue MPD A 502
ChainResidue
BARG280
ALYS438
AGLY439
AHOH612
AHOH652

site_idAC3
Number of Residues3
Detailsbinding site for residue MPD A 503
ChainResidue
AGLY140
AARG453
AMPD504

site_idAC4
Number of Residues2
Detailsbinding site for residue MPD A 504
ChainResidue
AARG453
AMPD503

site_idAC5
Number of Residues4
Detailsbinding site for residue MPD A 505
ChainResidue
APRO337
AARG436
BGLY55
BHOH974

site_idAC6
Number of Residues4
Detailsbinding site for residue MPD A 506
ChainResidue
AHOH758
BPRO337
BPRO434
BARG436

site_idAC7
Number of Residues4
Detailsbinding site for residue CU A 507
ChainResidue
AHIS97
ATRP133
AHIS135
AHIS446

site_idAC8
Number of Residues4
Detailsbinding site for residue CU A 508
ChainResidue
AHIS393
ACYS445
AHIS450
AMET455

site_idAC9
Number of Residues4
Detailsbinding site for residue CU A 509
ChainResidue
AHIS95
AHIS137
AHIS398
AHIS444

site_idAD1
Number of Residues4
Detailsbinding site for residue CU A 510
ChainResidue
AHIS95
AHIS97
AHIS396
AHIS398

site_idAD2
Number of Residues2
Detailsbinding site for residue CU A 511
ChainResidue
AMET192
AMPD501

site_idAD3
Number of Residues2
Detailsbinding site for residue CU A 512
ChainResidue
AMET293
AMET354

site_idAD4
Number of Residues2
Detailsbinding site for residue MPD B 501
ChainResidue
BPRO191
BARG453

site_idAD5
Number of Residues4
Detailsbinding site for residue MPD B 502
ChainResidue
BPRO342
BVAL343
BVAL344
BTHR345

site_idAD6
Number of Residues7
Detailsbinding site for residue MRD B 503
ChainResidue
ATHR212
AARG280
ATYR317
BLYS438
BGLY439
BHOH626
BHOH630

site_idAD7
Number of Residues4
Detailsbinding site for residue CU B 504
ChainResidue
BHIS97
BTRP133
BHIS135
BHIS446

site_idAD8
Number of Residues4
Detailsbinding site for residue CU B 505
ChainResidue
BHIS393
BCYS445
BHIS450
BMET455

site_idAD9
Number of Residues3
Detailsbinding site for residue CU B 506
ChainResidue
BHIS137
BHIS398
BHIS444

site_idAE1
Number of Residues4
Detailsbinding site for residue CU B 507
ChainResidue
BHIS95
BHIS97
BHIS396
BHIS398

site_idAE2
Number of Residues3
Detailsbinding site for residue CU B 508
ChainResidue
BMET296
BHIS303
BMET305

Functional Information from PROSITE/UniProt
site_idPS00080
Number of Residues12
DetailsMULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHiveHedrGM
ChainResidueDetails
AHIS444-MET455

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PDB entries from 2024-07-17

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