Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1O94

Ternary complex between trimethylamine dehydrogenase and electron transferring flavoprotein

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0010181	molecular_function	FMN binding
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
A	0050470	molecular_function	trimethylamine dehydrogenase activity
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0010181	molecular_function	FMN binding
B	0016491	molecular_function	oxidoreductase activity
B	0046872	molecular_function	metal ion binding
B	0050470	molecular_function	trimethylamine dehydrogenase activity
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0000166	molecular_function	nucleotide binding
C	0009055	molecular_function	electron transfer activity
D	0009055	molecular_function	electron transfer activity
D	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
D	0050660	molecular_function	flavin adenine dinucleotide binding
E	0000166	molecular_function	nucleotide binding
E	0009055	molecular_function	electron transfer activity
F	0009055	molecular_function	electron transfer activity
F	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
F	0050660	molecular_function	flavin adenine dinucleotide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE FMN A 1730

Chain	Residue
A	VAL27
A	ARG222
A	TRP264
A	ASP267
A	VAL297
A	ARG299
A	CYS320
A	ALA321
A	ARG322
A	PRO323
A	ILE352
A	PRO28
A	HOH2712
A	HOH2714
A	HOH2715
A	HIS29
A	CYS30
A	GLU59
A	TYR60
A	GLU103
A	TYR169
A	HIS172

site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ADP A 1731

Chain	Residue
A	VAL395
A	GLY396
A	GLY398
A	PRO399
A	SER400
A	ASP419
A	THR420
A	GLY426
A	HIS427
A	PRO469
A	MET470
A	ALA486
A	THR487
A	GLY488
A	GLY673
A	ASP674
A	HOH2402
A	HOH2488
A	HOH2716
A	HOH2717
A	HOH2718

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 A 1732

Chain	Residue
A	ARG322
A	ILE325
A	CYS345
A	ILE346
A	GLY347
A	CYS348
A	ASN349
A	CYS351
A	CYS364
A	THR365

site_id	AC4
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FMN B 1730

Chain	Residue
B	VAL27
B	PRO28
B	HIS29
B	CYS30
B	GLU59
B	TYR60
B	GLU103
B	TYR169
B	HIS172
B	ARG222
B	TRP264
B	ASP267
B	ALA268
B	VAL297
B	ARG299
B	CYS320
B	ALA321
B	ARG322
B	PRO323
B	ILE352
B	HOH2388
B	HOH2823
B	HOH2824

site_id	AC5
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ADP B 1731

Chain	Residue
B	VAL395
B	GLY396
B	GLY398
B	PRO399
B	SER400
B	ASP419
B	THR420
B	GLY426
B	HIS427
B	PRO469
B	MET470
B	ALA486
B	THR487
B	GLY488
B	GLY673
B	ASP674
B	HOH2825
B	HOH2826
B	HOH2827
B	HOH2828
B	HOH2829
B	HOH2830

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 B 1732

Chain	Residue
B	ILE325
B	CYS345
B	CYS348
B	ASN349
B	CYS351
B	CYS364
B	THR365
B	ARG322

site_id	AC7
Number of Residues	20
Details	BINDING SITE FOR RESIDUE AMP C 1236

Chain	Residue
C	ALA6
C	VAL7
C	LYS8
C	ASN36
C	ASP39
C	VAL62
C	SER63
C	VAL64
C	ALA118
C	GLY119
C	GLN121
C	SER122
C	TYR127
C	ALA128
C	SER129
C	THR130
C	HOH2113
C	HOH2114
C	HOH2177
C	HOH2178

site_id	AC8
Number of Residues	21
Details	BINDING SITE FOR RESIDUE AMP E 1237

Chain	Residue
E	ALA6
E	VAL7
E	LYS8
E	ASN36
E	ASP39
E	VAL62
E	SER63
E	VAL64
E	VAL100
E	ALA118
E	GLY119
E	GLN121
E	SER122
E	TYR127
E	ALA128
E	SER129
E	THR130
E	HOH2117
E	HOH2126
E	HOH2197
E	HOH2198

Functional Information from PROSITE/UniProt

site_id	PS00696
Number of Residues	27
Details	ETF_ALPHA Electron transfer flavoprotein alpha-subunit signature. LYVAmGISGsIQHmaGmkhvptIiAVN

Chain	Residue	Details
D	LEU262-ASN288

site_id	PS01065
Number of Residues	22
Details	ETF_BETA Electron transfer flavoprotein beta-subunit signature. IrRelEGGmlQeVeincPaVLT

Chain	Residue	Details
C	ILE160-THR181

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	34
Details	Binding site: {"evidences":[{"source":"PDB","id":"1DJN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DJQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O94","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O95","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2TMD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"1551870","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"620783","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1O94","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O95","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2TMD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PDB","id":"1DJQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2TMD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"S-6-FMN cysteine"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12567183","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1O94","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O95","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O96","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CLR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CLS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CLU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PDB","id":"1O94","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O95","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O96","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CLR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CLS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CLU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ps9

Chain	Residue	Details
A	TYR174
A	ASP260

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ps9

Chain	Residue	Details
B	TYR174
B	ASP260

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ps9

Chain	Residue	Details
A	HIS172
A	TYR169
A	ASP267

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ps9

Chain	Residue	Details
B	HIS172
B	TYR169
B	ASP267

site_id	MCSA1
Number of Residues	4
Details	M-CSA 114

Chain	Residue	Details
A	CYS30	activator, alter redox potential, covalently attached
A	TYR169	activator, alter redox potential, electrostatic stabiliser, hydrogen bond donor
A	HIS172	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
A	ASP267	electrostatic stabiliser

site_id	MCSA2
Number of Residues	4
Details	M-CSA 114

Chain	Residue	Details
B	CYS30	activator, alter redox potential, covalently attached
B	TYR169	activator, alter redox potential, electrostatic stabiliser, hydrogen bond donor
B	HIS172	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
B	ASP267	electrostatic stabiliser

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