Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4NXL

Dibenzothiophene monooxygenase (DszC) from Rhodococcus erythropolis

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003995molecular_functionacyl-CoA dehydrogenase activity
A0004497molecular_functionmonooxygenase activity
A0005737cellular_componentcytoplasm
A0006552biological_processL-leucine catabolic process
A0008470molecular_function3-methylbutanoyl-CoA dehydrogenase activity
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0018896biological_processdibenzothiophene catabolic process
A0050660molecular_functionflavin adenine dinucleotide binding
B0000166molecular_functionnucleotide binding
B0003995molecular_functionacyl-CoA dehydrogenase activity
B0004497molecular_functionmonooxygenase activity
B0005737cellular_componentcytoplasm
B0006552biological_processL-leucine catabolic process
B0008470molecular_function3-methylbutanoyl-CoA dehydrogenase activity
B0016491molecular_functionoxidoreductase activity
B0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
B0018896biological_processdibenzothiophene catabolic process
B0050660molecular_functionflavin adenine dinucleotide binding
C0000166molecular_functionnucleotide binding
C0003995molecular_functionacyl-CoA dehydrogenase activity
C0004497molecular_functionmonooxygenase activity
C0005737cellular_componentcytoplasm
C0006552biological_processL-leucine catabolic process
C0008470molecular_function3-methylbutanoyl-CoA dehydrogenase activity
C0016491molecular_functionoxidoreductase activity
C0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
C0018896biological_processdibenzothiophene catabolic process
C0050660molecular_functionflavin adenine dinucleotide binding
D0000166molecular_functionnucleotide binding
D0003995molecular_functionacyl-CoA dehydrogenase activity
D0004497molecular_functionmonooxygenase activity
D0005737cellular_componentcytoplasm
D0006552biological_processL-leucine catabolic process
D0008470molecular_function3-methylbutanoyl-CoA dehydrogenase activity
D0016491molecular_functionoxidoreductase activity
D0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
D0018896biological_processdibenzothiophene catabolic process
D0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PROSITE/UniProt
site_idPS00962
Number of Residues12
DetailsRIBOSOMAL_S2_1 Ribosomal protein S2 signature 1. IaQLIFANVYLG
ChainResidueDetails
AILE253-GLY264

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues424
DetailsRegion: {"description":"Helical N-terminus","evidences":[{"source":"PubMed","id":"24975806","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues432
DetailsRegion: {"description":"Central beta-barrel N-terminus","evidences":[{"source":"PubMed","id":"24975806","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues44
DetailsRegion: {"description":"Lid loop","evidences":[{"source":"UniProtKB","id":"A0A0C6DRW4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues696
DetailsRegion: {"description":"Helical C-terminus","evidences":[{"source":"PubMed","id":"24975806","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues52
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"A0A0C6DRW4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

PDB statisticsPDBj update infoContact PDBjnumon