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2I0F

Lumazine synthase RibH1 from Brucella abortus (Gene BruAb1_0785, Swiss-Prot entry Q57DY1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000906molecular_function6,7-dimethyl-8-ribityllumazine synthase activity
A0005829cellular_componentcytosol
A0009231biological_processriboflavin biosynthetic process
A0009349cellular_componentriboflavin synthase complex
A0016740molecular_functiontransferase activity
B0000906molecular_function6,7-dimethyl-8-ribityllumazine synthase activity
B0005829cellular_componentcytosol
B0009231biological_processriboflavin biosynthetic process
B0009349cellular_componentriboflavin synthase complex
B0016740molecular_functiontransferase activity
C0000906molecular_function6,7-dimethyl-8-ribityllumazine synthase activity
C0005829cellular_componentcytosol
C0009231biological_processriboflavin biosynthetic process
C0009349cellular_componentriboflavin synthase complex
C0016740molecular_functiontransferase activity
D0000906molecular_function6,7-dimethyl-8-ribityllumazine synthase activity
D0005829cellular_componentcytosol
D0009231biological_processriboflavin biosynthetic process
D0009349cellular_componentriboflavin synthase complex
D0016740molecular_functiontransferase activity
E0000906molecular_function6,7-dimethyl-8-ribityllumazine synthase activity
E0005829cellular_componentcytosol
E0009231biological_processriboflavin biosynthetic process
E0009349cellular_componentriboflavin synthase complex
E0016740molecular_functiontransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 301
ChainResidue
AALA157
BASP65
BASP68
BASN69

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 302
ChainResidue
AGLU73
BALA67
BGLU73

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CA E 303
ChainResidue
EGLU124

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CA A 304
ChainResidue
AGLU124

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 305
ChainResidue
BGLU40
BHOH546
BHOH547
ETYR45
EASP46

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00178
ChainResidueDetails
AHIS90
BHIS90
CHIS90
DHIS90
EHIS90

site_idSWS_FT_FI2
Number of Residues35
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00178
ChainResidueDetails
APHE22
BTHR82
BGLU87
BASN115
BHIS129
BLYS137
CPHE22
CALA53
CTHR82
CGLU87
CASN115
AALA53
CHIS129
CLYS137
DPHE22
DALA53
DTHR82
DGLU87
DASN115
DHIS129
DLYS137
EPHE22
ATHR82
EALA53
ETHR82
EGLU87
EASN115
EHIS129
ELYS137
AGLU87
AASN115
AHIS129
ALYS137
BPHE22
BALA53

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1rvv
ChainResidueDetails
AHIS90

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1rvv
ChainResidueDetails
BHIS90

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1rvv
ChainResidueDetails
CHIS90

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1rvv
ChainResidueDetails
DHIS90

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1rvv
ChainResidueDetails
EHIS90

221371

PDB entries from 2024-06-19

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