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

5MKM

Crystal Structure of Two-Domain Laccase mutant H165F from Streptomyces griseoflavus

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
A0052716molecular_functionhydroquinone:oxygen oxidoreductase activity
B0005507molecular_functioncopper ion binding
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
B0052716molecular_functionhydroquinone:oxygen oxidoreductase activity
C0005507molecular_functioncopper ion binding
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
C0052716molecular_functionhydroquinone:oxygen oxidoreductase activity
D0005507molecular_functioncopper ion binding
D0016491molecular_functionoxidoreductase activity
D0046872molecular_functionmetal ion binding
D0052716molecular_functionhydroquinone:oxygen oxidoreductase activity
E0005507molecular_functioncopper ion binding
E0016491molecular_functionoxidoreductase activity
E0046872molecular_functionmetal ion binding
E0052716molecular_functionhydroquinone:oxygen oxidoreductase activity
F0005507molecular_functioncopper ion binding
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 Residues5
Detailsbinding site for residue CU A 402
ChainResidue
AHIS103
AHIS105
AHIS157
AOXY403
BHIS290

site_idAC3
Number of Residues8
Detailsbinding site for residue OXY A 403
ChainResidue
AHIS103
AHIS157
AHIS159
ACU402
AHOH537
BHIS237
BHIS288
BHIS290

site_idAC4
Number of Residues4
Detailsbinding site for residue CU B 401
ChainResidue
BHIS232
BCYS289
BHIS294
BMET299

site_idAC5
Number of Residues5
Detailsbinding site for residue CU B 402
ChainResidue
BHIS103
BHIS105
BHIS157
CHIS290
CHOH626

site_idAC6
Number of Residues7
Detailsbinding site for residue O C 501
ChainResidue
AHIS237
AHIS288
AHIS290
CHIS103
CHIS157
CHIS159
CCU502

site_idAC7
Number of Residues5
Detailsbinding site for residue CU C 502
ChainResidue
AHIS290
CHIS103
CHIS105
CHIS157
CO501

site_idAC8
Number of Residues4
Detailsbinding site for residue CU C 503
ChainResidue
CHIS232
CCYS289
CHIS294
CMET299

site_idAC9
Number of Residues7
Detailsbinding site for residue EDO C 504
ChainResidue
AVAL258
CGLY152
CTYR153
CTRP154
CSER269
CHOH640
CHOH642

site_idAD1
Number of Residues7
Detailsbinding site for residue O D 501
ChainResidue
DHIS237
DHIS288
DHIS290
DHOH629
FHIS103
FHIS159
FCU401

site_idAD2
Number of Residues4
Detailsbinding site for residue CU D 502
ChainResidue
DHIS232
DCYS289
DHIS294
DMET299

site_idAD3
Number of Residues5
Detailsbinding site for residue CU D 503
ChainResidue
DHIS103
DHIS105
DHIS157
DOXY505
EHIS290

site_idAD4
Number of Residues10
Detailsbinding site for residue GOL D 504
ChainResidue
DGLY152
DTYR153
DTRP154
DARG245
DSER269
DHOH604
DHOH612
EGLN257
EVAL258
EILE259

site_idAD5
Number of Residues7
Detailsbinding site for residue OXY D 505
ChainResidue
DHIS103
DHIS157
DHIS159
DCU503
EHIS237
EHIS288
EHIS290

site_idAD6
Number of Residues4
Detailsbinding site for residue CU E 401
ChainResidue
EHIS232
ECYS289
EHIS294
EMET299

site_idAD7
Number of Residues4
Detailsbinding site for residue CU E 402
ChainResidue
EHIS103
EHIS105
EHIS157
FHIS290

site_idAD8
Number of Residues5
Detailsbinding site for residue CU F 401
ChainResidue
DHIS290
DO501
FHIS103
FHIS105
FHIS157

site_idAD9
Number of Residues4
Detailsbinding site for residue CU F 402
ChainResidue
FHIS232
FCYS289
FHIS294
FMET299

site_idAE1
Number of Residues2
Detailsbinding site for residue SO4 F 403
ChainResidue
FARG51
FTHR130

site_idAE2
Number of Residues4
Detailsbinding site for residue EDO F 404
ChainResidue
EASP268
FASN261
FLYS262
FILE263

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

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon