Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6EI9

Crystal structure of E. coli tRNA-dihydrouridine synthase B (DusB)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0002943biological_processtRNA dihydrouridine synthesis
A0008033biological_processtRNA processing
A0009314biological_processresponse to radiation
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0017150molecular_functiontRNA dihydrouridine synthase activity
A0050660molecular_functionflavin adenine dinucleotide binding
B0000049molecular_functiontRNA binding
B0002943biological_processtRNA dihydrouridine synthesis
B0008033biological_processtRNA processing
B0009314biological_processresponse to radiation
B0010181molecular_functionFMN binding
B0016491molecular_functionoxidoreductase activity
B0017150molecular_functiontRNA dihydrouridine synthase activity
B0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue FMN A 401
ChainResidue
AALA15
AASN200
AASP202
AGLY224
AARG225
AGOL402
AHOH506
AHOH527
APRO16
AMET17
AALA18
AGLN70
AASN97
ACYS100
ALYS139
AHIS169

site_idAC2
Number of Residues8
Detailsbinding site for residue GOL A 402
ChainResidue
AGLY99
ACYS100
ALYS139
AILE140
AARG141
AHIS169
APHE177
AFMN401

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 403
ChainResidue
AARG149
AGLU182
AASP184
AHOH525
BPRO249

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 A 404
ChainResidue
AGLU40
AVAL69
AASN86
ASER89
AHOH509

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 A 405
ChainResidue
APRO-3
AARG210
ALEU241
BHOH524

site_idAC6
Number of Residues1
Detailsbinding site for residue SO4 A 406
ChainResidue
ATYR276

site_idAC7
Number of Residues16
Detailsbinding site for residue FMN B 401
ChainResidue
BALA15
BPRO16
BMET17
BALA18
BGLN70
BLYS139
BPHE177
BASN200
BGLY201
BASP202
BGLY224
BARG225
BSO4403
BSO4406
BHOH503
BHOH534

site_idAC8
Number of Residues7
Detailsbinding site for residue GOL B 402
ChainResidue
BARG9
BTYR30
BGLU31
BARG187
BGLN191
BHOH537
BHOH565

site_idAC9
Number of Residues6
Detailsbinding site for residue SO4 B 403
ChainResidue
BGLY99
BCYS100
BPRO101
BARG141
BHIS169
BFMN401

site_idAD1
Number of Residues4
Detailsbinding site for residue SO4 B 404
ChainResidue
BPRO146
BGLU147
BHIS148
BARG149

site_idAD2
Number of Residues1
Detailsbinding site for residue SO4 B 405
ChainResidue
BGLN238

site_idAD3
Number of Residues4
Detailsbinding site for residue SO4 B 406
ChainResidue
BCYS100
BLYS103
BFMN401
BHOH511

site_idAD4
Number of Residues3
Detailsbinding site for residue EPE B 407
ChainResidue
BASP62
BGLU63
BSER89

Functional Information from PROSITE/UniProt
site_idPS01136
Number of Residues19
DetailsUPF0034 Uncharacterized protein family UPF0034 signature. IDINmGCPakk.Vnrkla.GS
ChainResidueDetails
AILE94-SER112

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q5SMC7, ECO:0000255|HAMAP-Rule:MF_02042
ChainResidueDetails
ACYS100
BCYS100

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P33371, ECO:0000255|HAMAP-Rule:MF_02042
ChainResidueDetails
APRO16
BGLY224
AGLN70
ALYS139
AASN200
AGLY224
BPRO16
BGLN70
BLYS139
BASN200

222036

PDB entries from 2024-07-03

PDB statisticsPDBj update infoContact PDBjnumon