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3EX8

Complex structure of bacillus subtilis RibG reduction mechanism in riboflavin biosynthesis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0008270molecular_functionzinc ion binding
A0008703molecular_function5-amino-6-(5-phosphoribosylamino)uracil reductase activity
A0008835molecular_functiondiaminohydroxyphosphoribosylaminopyrimidine deaminase activity
A0009231biological_processriboflavin biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0050661molecular_functionNADP binding
B0003824molecular_functioncatalytic activity
B0008270molecular_functionzinc ion binding
B0008703molecular_function5-amino-6-(5-phosphoribosylamino)uracil reductase activity
B0008835molecular_functiondiaminohydroxyphosphoribosylaminopyrimidine deaminase activity
B0009231biological_processriboflavin biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
B0050661molecular_functionNADP binding
C0003824molecular_functioncatalytic activity
C0008270molecular_functionzinc ion binding
C0008703molecular_function5-amino-6-(5-phosphoribosylamino)uracil reductase activity
C0008835molecular_functiondiaminohydroxyphosphoribosylaminopyrimidine deaminase activity
C0009231biological_processriboflavin biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
C0050661molecular_functionNADP binding
D0003824molecular_functioncatalytic activity
D0008270molecular_functionzinc ion binding
D0008703molecular_function5-amino-6-(5-phosphoribosylamino)uracil reductase activity
D0008835molecular_functiondiaminohydroxyphosphoribosylaminopyrimidine deaminase activity
D0009231biological_processriboflavin biosynthetic process
D0016491molecular_functionoxidoreductase activity
D0016787molecular_functionhydrolase activity
D0046872molecular_functionmetal ion binding
D0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 362
ChainResidue
AHIS49
ACYS74
ACYS83

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 362
ChainResidue
BHIS49
BGLU51
BCYS74
BCYS83
BHOH400

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 362
ChainResidue
CCYS74
CCYS83
CHOH383
CHIS49

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE AIF C 381
ChainResidue
CLYS151
CALA153
CSER167
CTRP169
CILE170
CTHR171
CARG176
CARG183
CTHR195
CASP199
CPRO201
CSER202
CLEU203
CARG206
CGLU290
CHOH382

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN D 362
ChainResidue
DHIS49
DCYS74
DCYS83

Functional Information from PROSITE/UniProt
site_idPS00903
Number of Residues39
DetailsCYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HAEvhAIhmagahaegadiyvtle................PCshygktppCaelI
ChainResidueDetails
AHIS49-ILE87

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues484
DetailsDomain: {"description":"CMP/dCMP-type deaminase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01083","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues572
DetailsRegion: {"description":"Deaminase"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues56
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues20
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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