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4BFA

Crystal structure of E. coli dihydrouridine synthase C (DusC)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0002943biological_processtRNA dihydrouridine synthesis
A0003723molecular_functionRNA binding
A0008033biological_processtRNA processing
A0010181molecular_functionFMN binding
A0010467biological_processgene expression
A0016491molecular_functionoxidoreductase activity
A0017150molecular_functiontRNA dihydrouridine synthase activity
A0050660molecular_functionflavin adenine dinucleotide binding
A0071461biological_processcellular response to redox state
A0102262molecular_functiontRNA-dihydrouridine16 synthase activity
B0000049molecular_functiontRNA binding
B0002943biological_processtRNA dihydrouridine synthesis
B0003723molecular_functionRNA binding
B0008033biological_processtRNA processing
B0010181molecular_functionFMN binding
B0010467biological_processgene expression
B0016491molecular_functionoxidoreductase activity
B0017150molecular_functiontRNA dihydrouridine synthase activity
B0050660molecular_functionflavin adenine dinucleotide binding
B0071461biological_processcellular response to redox state
B0102262molecular_functiontRNA-dihydrouridine16 synthase activity
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE FMN A 1316
ChainResidue
AALA6
AHIS168
ATYR176
AASN200
AGLY201
AGLU202
AGLY224
AARG225
AHOH2132
AHOH2215
AHOH2219
APRO7
BARG177
AMET8
AGLU9
APHE33
AGLN68
AASN95
ACYS98
ALYS139

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FMN B 1316
ChainResidue
AARG177
BALA6
BPRO7
BMET8
BGLU9
BPHE33
BGLN68
BASN95
BLYS139
BHIS168
BTYR176
BASN200
BGLY201
BGLU202
BGLY224
BARG225
BHOH2132
BHOH2196
BHOH2199

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1317
ChainResidue
ATRP183
AGLN211
AHOH2196
AHOH2216
AHOH2303
BARG281
BTHR288

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1318
ChainResidue
AARG225
AASN229
ATYR279
ALYS282
AHOH2236
AHOH2285
BGLU179

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 1317
ChainResidue
AALA132
BARG2
BASP27
BTRP90

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 1318
ChainResidue
BASP155
BGLN158
BGLN159
BHOH2306

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NO3 A 1319
ChainResidue
AASP182
ATRP183
AGLN184
AHOH2303
AHOH2304
BARG281
BPHE291
BGLN292
BARG295

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 B 1319
ChainResidue
AARG281
AGLN292
AARG295
AHOH2289
BILE181
BASP182
BTRP183
BGLN184

Functional Information from PROSITE/UniProt
site_idPS01136
Number of Residues19
DetailsUPF0034 Uncharacterized protein family UPF0034 signature. VDLNcGCPskt.Vngsgg.GA
ChainResidueDetails
AVAL92-ALA110

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q5SMC7","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"25902496","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23908023","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25902496","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3W9Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BF9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BFA","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsSite: {"description":"Interacts with tRNA; defines subfamily-specific binding signature","evidences":[{"source":"PubMed","id":"25902496","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsSite: {"description":"Interacts with tRNA","evidences":[{"source":"PubMed","id":"25902496","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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