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

1LUC

BACTERIAL LUCIFERASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0008218biological_processbioluminescence
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0047646molecular_functionalkanal monooxygenase (FMN-linked) activity
B0004497molecular_functionmonooxygenase activity
B0005829cellular_componentcytosol
B0008218biological_processbioluminescence
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0047646molecular_functionalkanal monooxygenase (FMN-linked) activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 2001
ChainResidue
AGLU19
AHOH3101
AHOH3174
AHOH3175
AHOH3176
AHOH3177

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 2002
ChainResidue
BHOH3152
BHOH3178
BHOH3179
AASP346
BGLU237
BHOH3151

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 2003
ChainResidue
AHOH3335
AHOH3352
AHOH3380
AHOH3418
AHOH3419
AHOH3486

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 2500
ChainResidue
ALEU24
AGLY28
AHIS61
ALEU62
AHOH3187

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 2501
ChainResidue
AHIS82
BPHE116
BPHE117
BHOH3068

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 2502
ChainResidue
AARG125
AASP129
ATHR179
ATRP182
AHOH3614

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 2503
ChainResidue
ALYS341
BASN233
BHOH3044
BHOH3560
BHOH3658

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 2504
ChainResidue
APRO154
AILE156
BALA112
BASP113
BPHE116
BHOH3164
BHOH3587

Functional Information from PROSITE/UniProt
site_idPS00494
Number of Residues26
DetailsBACTERIAL_LUCIFERASE Bacterial luciferase subunits signature. GLPMiLsWiintheKkaqldlYnevA
ChainResidueDetails
AGLY187-ALA212
BGLY187-ALA212

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 9402752, 10194361
ChainResidueDetails
AHIS44
AHIS45

site_idMCSA1
Number of Residues5
DetailsM-CSA 132
ChainResidueDetails
AHIS44activator, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor
AHIS45electrostatic stabiliser, polar/non-polar interaction
ACYS106electrostatic stabiliser
AASP113electrostatic stabiliser, hydrogen bond acceptor
ASER227electrostatic stabiliser, hydrogen bond donor

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon