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2O7P

The crystal structure of RibD from Escherichia coli in complex with the oxidised NADP+ cofactor in the active site of the reductase domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
B0000166molecular_functionnucleotide 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
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE NAP A 402
ChainResidue
ALYS152
ATHR196
AASP200
AASP233
ASER234
AARG237
AHIS278
ALEU279
ALEU281
AALA300
AGLY301
ATHR161
APRO302
ATHR303
ALEU304
AALA307
AALA162
AMSE163
AALA164
ATRP170
ASER193
ASER194
AALA195

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAP B 1402
ChainResidue
BLYS152
BTRP170
BSER193
BSER194
BALA195
BTHR196
BASP200
BILE232
BASP233
BSER234
BARG237
BHIS278
BLEU279
BLEU281
BGLU299
BALA300
BGLY301
BPRO302
BTHR303
BLEU304
BALA307

Functional Information from PROSITE/UniProt
site_idPS00903
Number of Residues39
DetailsCYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HAEvhALrmagekakgatayvtle................PCshhgrtppCcdaL
ChainResidueDetails
AHIS50-LEU88

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU52
BGLU52

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS50
ACYS75
ACYS84
BHIS50
BCYS75
BCYS84

site_idSWS_FT_FI3
Number of Residues22
DetailsBINDING:
ChainResidueDetails
ATHR161
AGLU299
AGLY301
BTHR161
BSER168
BTRP170
BARG184
BTHR196
BASP200
BLEU204
BARG207
ASER168
BSER234
BGLU299
BGLY301
ATRP170
AARG184
ATHR196
AASP200
ALEU204
AARG207
ASER234

224201

PDB entries from 2024-08-28

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