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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
A0008033biological_processtRNA processing
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0017150molecular_functiontRNA dihydrouridine synthase activity
A0050660molecular_functionflavin adenine dinucleotide binding
A0102262molecular_functiontRNA-dihydrouridine16 synthase activity
B0000049molecular_functiontRNA binding
B0002943biological_processtRNA dihydrouridine synthesis
B0008033biological_processtRNA processing
B0010181molecular_functionFMN binding
B0016491molecular_functionoxidoreductase activity
B0017150molecular_functiontRNA dihydrouridine synthase activity
B0050660molecular_functionflavin adenine dinucleotide binding
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 Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q5SMC7, ECO:0000305|PubMed:25902496
ChainResidueDetails
ACYS98
BCYS98

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:23908023, ECO:0000269|PubMed:25902496, ECO:0007744|PDB:3W9Z, ECO:0007744|PDB:4BF9, ECO:0007744|PDB:4BFA
ChainResidueDetails
APRO7
BGLY224
AGLN68
ALYS139
AASN200
AGLY224
BPRO7
BGLN68
BLYS139
BASN200

site_idSWS_FT_FI3
Number of Residues8
DetailsSITE: Interacts with tRNA; defines subfamily-specific binding signature => ECO:0000269|PubMed:25902496
ChainResidueDetails
AARG35
AARG272
ALYS274
AARG295
BARG35
BARG272
BLYS274
BARG295

site_idSWS_FT_FI4
Number of Residues6
DetailsSITE: Interacts with tRNA => ECO:0000269|PubMed:25902496
ChainResidueDetails
AASN95
ATYR176
ATYR279
BASN95
BTYR176
BTYR279

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PDB entries from 2024-07-17

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