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3W9Z

Crystal structure of DusC

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0002943biological_processtRNA dihydrouridine synthesis
A0006725biological_processobsolete cellular aromatic compound metabolic process
A0008033biological_processtRNA processing
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0017150molecular_functiontRNA dihydrouridine synthase activity
A0050660molecular_functionflavin adenine dinucleotide binding
A0102262molecular_functiontRNA-dihydrouridine16 synthase activity
A1901360biological_processobsolete organic cyclic compound metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE FMN A 401
ChainResidue
AALA6
AHIS168
ATYR176
AASN200
AGLY201
AGLU202
AGLY224
AARG225
AHOH501
AHOH513
APRO7
AMET8
AGLU9
APHE33
AGLN68
AASN95
ACYS98
ALYS139

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
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q5SMC7, ECO:0000305|PubMed:25902496
ChainResidueDetails
ACYS98

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:23908023, ECO:0000269|PubMed:25902496, ECO:0007744|PDB:3W9Z, ECO:0007744|PDB:4BF9, ECO:0007744|PDB:4BFA
ChainResidueDetails
APRO7
AGLN68
ALYS139
AASN200
AGLY224

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Interacts with tRNA; defines subfamily-specific binding signature => ECO:0000269|PubMed:25902496
ChainResidueDetails
AARG35
AARG272
ALYS274
AARG295

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: Interacts with tRNA => ECO:0000269|PubMed:25902496
ChainResidueDetails
AASN95
ATYR176
ATYR279

221371

PDB entries from 2024-06-19

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