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4G3M

Complex Structure of Bacillus subtilis RibG: The Deamination Process 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 Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
AHIS49
AGLU51
ACYS74
ACYS83

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE AI9 A 402
ChainResidue
AARG176
AARG183
AASP199
APRO201
ASER202
ALEU203
ATHR204
AARG206
AGLU290
AHOH511
AHOH546
AHOH603
ALYS151
AALA153
ASER167
AILE170
ATHR171

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 401
ChainResidue
BHIS49
BCYS74
BCYS83
BAOF402

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE AOF B 402
ChainResidue
BASN23
BVAL26
BHIS42
BHIS49
BALA50
BGLU51
BCYS74
BHIS76
BLYS79
BTHR80
BCYS83
BASP101
BASN103
BPHE137
BZN401
BHOH503
BHOH533

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AI9 B 403
ChainResidue
BLYS151
BALA153
BSER167
BILE170
BTHR171
BARG176
BARG183
BASP199
BPRO201
BSER202
BLEU203
BARG206
BHOH568

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 401
ChainResidue
CHIS49
CCYS74
CCYS83
CAOF402

site_idAC7
Number of Residues16
DetailsBINDING SITE FOR RESIDUE AOF C 402
ChainResidue
CASN23
CPRO24
CVAL26
CHIS42
CHIS49
CALA50
CGLU51
CCYS74
CGLY78
CLYS79
CTHR80
CASP101
CPHE137
CZN401
CHOH550
CHOH561

site_idAC8
Number of Residues16
DetailsBINDING SITE FOR RESIDUE AI9 C 403
ChainResidue
CLYS151
CALA153
CSER167
CTRP169
CILE170
CTHR171
CARG176
CARG183
CASP199
CPRO201
CSER202
CLEU203
CARG206
CGLU290
CHOH506
CHOH549

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 401
ChainResidue
DHIS49
DCYS74
DCYS83
DAOF402

site_idBC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE AOF D 402
ChainResidue
DHIS49
DALA50
DGLU51
DCYS74
DHIS76
DGLY78
DLYS79
DTHR80
DCYS83
DASP101
DPHE137
DZN401
DHOH530
DHOH549
DASN23
DPRO24
DVAL26
DHIS42

site_idBC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE AI9 D 403
ChainResidue
DLYS151
DALA153
DILE170
DTHR171
DARG176
DARG183
DASP199
DPRO201
DSER202
DLEU203
DARG206
DGLU290

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

239492

PDB entries from 2025-07-30

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