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2D5N

Crystal structure of a bifunctional deaminase and reductase involved 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 1360
ChainResidue
AHIS49
AGLU51
ACYS74
ACYS83

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1360
ChainResidue
BHIS49
BGLU51
BCYS74
BCYS83

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 1360
ChainResidue
CGLU51
CCYS74
CCYS83
CHIS49

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 1360
ChainResidue
DHIS49
DGLU51
DCYS74
DCYS83

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE NDP B 381
ChainResidue
BALA152
BALA153
BILE160
BGLY165
BGLY192
BVAL193
BGLY194
BTHR195
BASP199
BTHR221
BILE270
BGLU290
BGLY292
BSER293
BALA294
BVAL295
BSER298
BHOH1407
BHOH1424

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 Residues4
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU51
BGLU51
CGLU51
DGLU51

site_idSWS_FT_FI2
Number of Residues36
DetailsBINDING:
ChainResidueDetails
AHIS49
BHIS49
BCYS74
BCYS83
BALA153
BTRP169
BTHR195
BASP199
BTHR221
BGLY292
CHIS49
ACYS74
CCYS74
CCYS83
CALA153
CTRP169
CTHR195
CASP199
CTHR221
CGLY292
DHIS49
DCYS74
ACYS83
DCYS83
DALA153
DTRP169
DTHR195
DASP199
DTHR221
DGLY292
AALA153
ATRP169
ATHR195
AASP199
ATHR221
AGLY292

site_idSWS_FT_FI3
Number of Residues20
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER167
BGLU290
CSER167
CARG183
CLEU203
CARG206
CGLU290
DSER167
DARG183
DLEU203
DARG206
AARG183
DGLU290
ALEU203
AARG206
AGLU290
BSER167
BARG183
BLEU203
BARG206

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PDB entries from 2025-06-18

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