Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6RHQ

Crystal Structure of Two-Domain Laccase mutant I170A from Streptomyces griseoflavus

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0005886cellular_componentplasma membrane
A0006826biological_processiron ion transport
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
A0052716molecular_functionhydroquinone:oxygen oxidoreductase activity
B0005507molecular_functioncopper ion binding
B0005886cellular_componentplasma membrane
B0006826biological_processiron ion transport
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
B0052716molecular_functionhydroquinone:oxygen oxidoreductase activity
C0005507molecular_functioncopper ion binding
C0005886cellular_componentplasma membrane
C0006826biological_processiron ion transport
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
C0052716molecular_functionhydroquinone:oxygen oxidoreductase activity
D0005507molecular_functioncopper ion binding
D0005886cellular_componentplasma membrane
D0006826biological_processiron ion transport
D0016491molecular_functionoxidoreductase activity
D0046872molecular_functionmetal ion binding
D0052716molecular_functionhydroquinone:oxygen oxidoreductase activity
E0005507molecular_functioncopper ion binding
E0005886cellular_componentplasma membrane
E0006826biological_processiron ion transport
E0016491molecular_functionoxidoreductase activity
E0046872molecular_functionmetal ion binding
E0052716molecular_functionhydroquinone:oxygen oxidoreductase activity
F0005507molecular_functioncopper ion binding
F0005886cellular_componentplasma membrane
F0006826biological_processiron ion transport
F0016491molecular_functionoxidoreductase activity
F0046872molecular_functionmetal ion binding
F0052716molecular_functionhydroquinone:oxygen oxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CU A 401
ChainResidue
AHIS232
ACYS289
AHIS294
AMET299

site_idAC2
Number of Residues4
Detailsbinding site for residue CU A 402
ChainResidue
AHIS237
AHIS288
AHOH525
CHIS159

site_idAC3
Number of Residues5
Detailsbinding site for residue CU A 403
ChainResidue
AHIS237
CHIS103
CHIS105
CCU401
AHIS235

site_idAC4
Number of Residues5
Detailsbinding site for residue CU A 404
ChainResidue
AHIS103
AHIS105
AHIS157
BHIS290
BHOH527

site_idAC5
Number of Residues4
Detailsbinding site for residue CU B 401
ChainResidue
BHIS232
BCYS289
BHIS294
BMET299

site_idAC6
Number of Residues5
Detailsbinding site for residue CU B 402
ChainResidue
AHIS159
BHIS237
BHIS288
BCU403
BHOH527

site_idAC7
Number of Residues6
Detailsbinding site for residue CU B 403
ChainResidue
AHIS103
AHOH528
BHIS235
BHIS237
BCU402
BHOH527

site_idAC8
Number of Residues5
Detailsbinding site for residue CU B 404
ChainResidue
BHIS103
BHIS105
BHIS157
CHIS290
CHOH523

site_idAC9
Number of Residues6
Detailsbinding site for residue CU C 401
ChainResidue
AHIS290
ACU403
AHOH525
CHIS103
CHIS105
CHIS157

site_idAD1
Number of Residues4
Detailsbinding site for residue CU C 402
ChainResidue
CHIS232
CCYS289
CHIS294
CMET299

site_idAD2
Number of Residues4
Detailsbinding site for residue CU C 403
ChainResidue
BHIS159
CHIS237
CHIS288
CHOH523

site_idAD3
Number of Residues5
Detailsbinding site for residue CU C 404
ChainResidue
BHIS103
BHIS105
BHOH501
CHIS235
CHIS237

site_idAD4
Number of Residues4
Detailsbinding site for residue CU D 401
ChainResidue
DHIS232
DCYS289
DHIS294
DMET299

site_idAD5
Number of Residues4
Detailsbinding site for residue CU D 402
ChainResidue
DHIS237
DHIS288
DHOH567
FHIS159

site_idAD6
Number of Residues6
Detailsbinding site for residue CU D 403
ChainResidue
DHIS235
DHIS237
DHOH567
FHIS103
FHIS105
FCU401

site_idAD7
Number of Residues5
Detailsbinding site for residue CU D 404
ChainResidue
DHIS103
DHIS105
DHIS157
DHOH537
EHIS290

site_idAD8
Number of Residues7
Detailsbinding site for residue GOL D 405
ChainResidue
DGLY152
DTYR153
DVAL180
DARG181
DASP185
DARG245
DTHR246

site_idAD9
Number of Residues4
Detailsbinding site for residue CU E 401
ChainResidue
EHIS232
ECYS289
EHIS294
EMET299

site_idAE1
Number of Residues5
Detailsbinding site for residue CU E 402
ChainResidue
DHIS159
DHOH537
EHIS237
EMET286
EHIS288

site_idAE2
Number of Residues5
Detailsbinding site for residue CU E 403
ChainResidue
DHIS103
DHIS105
DHOH503
EHIS235
EHIS237

site_idAE3
Number of Residues5
Detailsbinding site for residue CU E 404
ChainResidue
EHIS157
FHIS290
FHOH501
EHIS103
EHIS105

site_idAE4
Number of Residues1
Detailsbinding site for residue SO4 E 405
ChainResidue
EARG134

site_idAE5
Number of Residues4
Detailsbinding site for residue GOL E 406
ChainResidue
EARG50
ELEU79
EILE80
EGLU81

site_idAE6
Number of Residues6
Detailsbinding site for residue CU F 401
ChainResidue
DHIS290
DCU403
DHOH567
FHIS103
FHIS105
FHIS157

site_idAE7
Number of Residues4
Detailsbinding site for residue CU F 402
ChainResidue
FHIS232
FCYS289
FHIS294
FMET299

site_idAE8
Number of Residues4
Detailsbinding site for residue CU F 403
ChainResidue
EHIS159
FHIS237
FHIS288
FHOH501

site_idAE9
Number of Residues4
Detailsbinding site for residue CU F 404
ChainResidue
EHIS103
EHOH517
FHIS235
FHIS237

site_idAF1
Number of Residues4
Detailsbinding site for residue SO4 F 405
ChainResidue
DGLY279
FARG134
FARG147
FHOH525

Functional Information from PROSITE/UniProt
site_idPS00080
Number of Residues12
DetailsMULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHvqsHsdmGM
ChainResidueDetails
AHIS288-MET299

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon