Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4DOY

Crystal structure of Dibenzothiophene desulfurization enzyme C

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003995	molecular_function	acyl-CoA dehydrogenase activity
A	0004497	molecular_function	monooxygenase activity
A	0005737	cellular_component	cytoplasm
A	0006552	biological_process	L-leucine catabolic process
A	0008470	molecular_function	3-methylbutanoyl-CoA dehydrogenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
A	0018896	biological_process	dibenzothiophene catabolic process
A	0050660	molecular_function	flavin adenine dinucleotide binding
B	0000166	molecular_function	nucleotide binding
B	0003995	molecular_function	acyl-CoA dehydrogenase activity
B	0004497	molecular_function	monooxygenase activity
B	0005737	cellular_component	cytoplasm
B	0006552	biological_process	L-leucine catabolic process
B	0008470	molecular_function	3-methylbutanoyl-CoA dehydrogenase activity
B	0016491	molecular_function	oxidoreductase activity
B	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
B	0018896	biological_process	dibenzothiophene catabolic process
B	0050660	molecular_function	flavin adenine dinucleotide binding
C	0000166	molecular_function	nucleotide binding
C	0003995	molecular_function	acyl-CoA dehydrogenase activity
C	0004497	molecular_function	monooxygenase activity
C	0005737	cellular_component	cytoplasm
C	0006552	biological_process	L-leucine catabolic process
C	0008470	molecular_function	3-methylbutanoyl-CoA dehydrogenase activity
C	0016491	molecular_function	oxidoreductase activity
C	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
C	0018896	biological_process	dibenzothiophene catabolic process
C	0050660	molecular_function	flavin adenine dinucleotide binding
D	0000166	molecular_function	nucleotide binding
D	0003995	molecular_function	acyl-CoA dehydrogenase activity
D	0004497	molecular_function	monooxygenase activity
D	0005737	cellular_component	cytoplasm
D	0006552	biological_process	L-leucine catabolic process
D	0008470	molecular_function	3-methylbutanoyl-CoA dehydrogenase activity
D	0016491	molecular_function	oxidoreductase activity
D	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
D	0018896	biological_process	dibenzothiophene catabolic process
D	0050660	molecular_function	flavin adenine dinucleotide binding
E	0000166	molecular_function	nucleotide binding
E	0003995	molecular_function	acyl-CoA dehydrogenase activity
E	0004497	molecular_function	monooxygenase activity
E	0005737	cellular_component	cytoplasm
E	0006552	biological_process	L-leucine catabolic process
E	0008470	molecular_function	3-methylbutanoyl-CoA dehydrogenase activity
E	0016491	molecular_function	oxidoreductase activity
E	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
E	0018896	biological_process	dibenzothiophene catabolic process
E	0050660	molecular_function	flavin adenine dinucleotide binding
F	0000166	molecular_function	nucleotide binding
F	0003995	molecular_function	acyl-CoA dehydrogenase activity
F	0004497	molecular_function	monooxygenase activity
F	0005737	cellular_component	cytoplasm
F	0006552	biological_process	L-leucine catabolic process
F	0008470	molecular_function	3-methylbutanoyl-CoA dehydrogenase activity
F	0016491	molecular_function	oxidoreductase activity
F	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
F	0018896	biological_process	dibenzothiophene catabolic process
F	0050660	molecular_function	flavin adenine dinucleotide binding
G	0000166	molecular_function	nucleotide binding
G	0003995	molecular_function	acyl-CoA dehydrogenase activity
G	0004497	molecular_function	monooxygenase activity
G	0005737	cellular_component	cytoplasm
G	0006552	biological_process	L-leucine catabolic process
G	0008470	molecular_function	3-methylbutanoyl-CoA dehydrogenase activity
G	0016491	molecular_function	oxidoreductase activity
G	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
G	0018896	biological_process	dibenzothiophene catabolic process
G	0050660	molecular_function	flavin adenine dinucleotide binding
H	0000166	molecular_function	nucleotide binding
H	0003995	molecular_function	acyl-CoA dehydrogenase activity
H	0004497	molecular_function	monooxygenase activity
H	0005737	cellular_component	cytoplasm
H	0006552	biological_process	L-leucine catabolic process
H	0008470	molecular_function	3-methylbutanoyl-CoA dehydrogenase activity
H	0016491	molecular_function	oxidoreductase activity
H	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
H	0018896	biological_process	dibenzothiophene catabolic process
H	0050660	molecular_function	flavin adenine dinucleotide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 500

Chain	Residue
A	LEU61
A	ALA71
A	ASP72
A	GLN324
A	HOH718
A	HOH794

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL B 501

Chain	Residue
B	TRP73
B	GLN324
B	TRP327
B	HOH665
B	HOH728
B	HOH779
B	HOH833
B	HOH945
B	LEU61
B	ALA71
B	ASP72

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 502

Chain	Residue
B	TRP205
B	HIS391
B	HOH744
E	ALA369

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 500

Chain	Residue
C	LEU61
C	ALA71
C	ASP72
C	GLN324
C	HOH790
C	HOH809
C	HOH931

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL D 501

Chain	Residue
D	ASP72
D	GLN324
D	GOL502
D	HOH804

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 502

Chain	Residue
D	LEU61
D	ALA71
D	TRP73
D	GOL501
D	HOH913

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL E 501

Chain	Residue
E	LEU61
E	ALA71
E	ASP72
E	TRP73
E	GLN324
E	HOH762
E	HOH798

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL E 502

Chain	Residue
E	TRP205
E	THR387
E	HOH796

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL F 500

Chain	Residue
F	LEU61
F	ALA71
F	ASP72
F	TRP73
F	GLN324
F	TRP327
F	HOH792
F	HOH863

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL G 501

Chain	Residue
G	LEU61
G	ALA71
G	ASP72
G	TRP73
G	GLN324
G	TRP327

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL G 502

Chain	Residue
G	TRP205
G	THR387

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL H 501

Chain	Residue
H	LEU61
H	ALA71
H	TRP73
H	GLN324
H	TRP327

site_id	BC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL H 502

Chain	Residue
H	TRP205

Functional Information from PROSITE/UniProt

site_id	PS00962
Number of Residues	12
Details	RIBOSOMAL_S2_1 Ribosomal protein S2 signature 1. IaQLIFANVYLG

Chain	Residue	Details
A	ILE253-GLY264

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	88
Details	Region: {"description":"First lid loop","evidences":[{"source":"UniProtKB","id":"A0A0C6DRW4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	120
Details	Region: {"description":"Second lid loop","evidences":[{"source":"PubMed","id":"24470304","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24470304","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	56
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A0C6DRW4","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"24470304","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	48
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A0C6DRW4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)