Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4N8U

Two-Domain Laccase from Streptomyces viridochromogenes at 2.4 A resolution AC629

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 401
ChainResidue
AHIS228
ACYS285
AHIS290
AMET295

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 402
ChainResidue
AHIS233
AHIS284
AHOH517
BHIS155

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU A 403
ChainResidue
AHIS153
CHIS286
AHIS101

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 404
ChainResidue
ATYR226

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 405
ChainResidue
AGLY180

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 401
ChainResidue
BHIS228
BCYS285
BHIS290
BMET295

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU B 402
ChainResidue
BHIS233
BHIS284
CHIS155

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 403
ChainResidue
AHIS286
AHOH517
BHIS101
BHIS153

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE TRS B 404
ChainResidue
BARG167
BASP194
BMET195
BTYR226
BHOH521

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 405
ChainResidue
BPRO74
BLEU75

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 406
ChainResidue
BARG46
BHIS47

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 401
ChainResidue
CHIS228
CCYS285
CHIS290
CMET295

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU C 402
ChainResidue
AHIS155
CHIS233
CHIS284

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU C 403
ChainResidue
BHIS231
BHIS286
BHOH519
CHIS101
CHIS153

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL C 404
ChainResidue
CTYR226
CTYR227

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL C 405
ChainResidue
AILE107
AASN115
CGLY279
CALA280
CPRO309
CGLY310

Functional Information from PROSITE/UniProt
site_idPS00080
Number of Residues12
DetailsMULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHvqsHsdmGM
ChainResidueDetails
AHIS284-MET295

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon