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1T13

Crystal Structure Of Lumazine Synthase From Brucella Abortus Bound To 5-nitro-6-(D-ribitylamino)-2,4(1H,3H) pyrimidinedione

Functional Information from GO Data
ChainGOidnamespacecontents
A0000906molecular_function6,7-dimethyl-8-ribityllumazine synthase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009231biological_processriboflavin biosynthetic process
A0009349cellular_componentriboflavin synthase complex
A0016740molecular_functiontransferase activity
B0000906molecular_function6,7-dimethyl-8-ribityllumazine synthase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0009231biological_processriboflavin biosynthetic process
B0009349cellular_componentriboflavin synthase complex
B0016740molecular_functiontransferase activity
C0000906molecular_function6,7-dimethyl-8-ribityllumazine synthase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0009231biological_processriboflavin biosynthetic process
C0009349cellular_componentriboflavin synthase complex
C0016740molecular_functiontransferase activity
D0000906molecular_function6,7-dimethyl-8-ribityllumazine synthase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0009231biological_processriboflavin biosynthetic process
D0009349cellular_componentriboflavin synthase complex
D0016740molecular_functiontransferase activity
E0000906molecular_function6,7-dimethyl-8-ribityllumazine synthase activity
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0009231biological_processriboflavin biosynthetic process
E0009349cellular_componentriboflavin synthase complex
E0016740molecular_functiontransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 190
ChainResidue
AILE82
AASP83
AGLY84
AGLY85
AILE86
ATYR87

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 191
ChainResidue
BGLY85
BILE86
BTYR87
BILE82
BASP83
BGLY84

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 C 192
ChainResidue
CASP83
CGLY84
CGLY85
CILE86
CTYR87
CINI202

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 D 193
ChainResidue
DASP83
DGLY84
DGLY85
DILE86
DTYR87

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 E 194
ChainResidue
EILE82
EASP83
EGLY84
EGLY85
EILE86
ETYR87
EINI201

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE INI E 201
ChainResidue
DLEU112
DSER113
EALA20
ETRP22
EGLY55
EALA56
ETYR57
EGLU58
EPHE80
EVAL81
EILE82
EPO4194
EHOH2110

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE INI C 202
ChainResidue
BLEU112
BSER113
CALA20
CTRP22
CGLY55
CALA56
CTYR57
CGLU58
CPHE80
CVAL81
CILE82
CPO4192

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE INI A 203
ChainResidue
AALA20
ATRP22
AGLY55
AALA56
ATYR57
AGLU58
APHE80
AVAL81
AILE82
AHOH2023
ELEU112
ESER113

site_idAC9
Number of Residues11
DetailsBINDING SITE FOR RESIDUE INI D 204
ChainResidue
CLEU112
CSER113
DALA20
DTRP22
DGLY55
DALA56
DTYR57
DGLU58
DPHE80
DVAL81
DILE82

site_idBC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE INI B 205
ChainResidue
ALEU112
ASER113
BALA20
BTRP22
BGLY55
BALA56
BTYR57
BGLU58
BPHE80
BVAL81
BILE82
BHOH2052

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00178
ChainResidueDetails
AARG88
BARG88
CARG88
DARG88
EARG88

site_idSWS_FT_FI2
Number of Residues25
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00178
ChainResidueDetails
ATRP22
BTRP22
BALA56
BPHE80
BSER113
BHIS124
CTRP22
CALA56
CPHE80
CSER113
CHIS124
DTRP22
DALA56
DPHE80
DSER113
DHIS124
ETRP22
EALA56
EPHE80
ESER113
EHIS124
AALA56
APHE80
ASER113
AHIS124

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PDB entries from 2024-06-12

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