Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1QG6

CRYSTAL STRUCTURE OF E. COLI ENOYL ACYL CARRIER PROTEIN REDUCTASE IN COMPLEX WITH NAD AND TRICLOSAN

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0006633	biological_process	fatty acid biosynthetic process
A	0008610	biological_process	lipid biosynthetic process
A	0009102	biological_process	biotin biosynthetic process
A	0016020	cellular_component	membrane
A	0030497	biological_process	fatty acid elongation
A	0032991	cellular_component	protein-containing complex
A	0042802	molecular_function	identical protein binding
A	0051289	biological_process	protein homotetramerization
A	0070404	molecular_function	NADH binding
A	1902494	cellular_component	catalytic complex
B	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
B	0005515	molecular_function	protein binding
B	0005829	cellular_component	cytosol
B	0006633	biological_process	fatty acid biosynthetic process
B	0008610	biological_process	lipid biosynthetic process
B	0009102	biological_process	biotin biosynthetic process
B	0016020	cellular_component	membrane
B	0030497	biological_process	fatty acid elongation
B	0032991	cellular_component	protein-containing complex
B	0042802	molecular_function	identical protein binding
B	0051289	biological_process	protein homotetramerization
B	0070404	molecular_function	NADH binding
B	1902494	cellular_component	catalytic complex
C	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
C	0005515	molecular_function	protein binding
C	0005829	cellular_component	cytosol
C	0006633	biological_process	fatty acid biosynthetic process
C	0008610	biological_process	lipid biosynthetic process
C	0009102	biological_process	biotin biosynthetic process
C	0016020	cellular_component	membrane
C	0030497	biological_process	fatty acid elongation
C	0032991	cellular_component	protein-containing complex
C	0042802	molecular_function	identical protein binding
C	0051289	biological_process	protein homotetramerization
C	0070404	molecular_function	NADH binding
C	1902494	cellular_component	catalytic complex
D	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
D	0005515	molecular_function	protein binding
D	0005829	cellular_component	cytosol
D	0006633	biological_process	fatty acid biosynthetic process
D	0008610	biological_process	lipid biosynthetic process
D	0009102	biological_process	biotin biosynthetic process
D	0016020	cellular_component	membrane
D	0030497	biological_process	fatty acid elongation
D	0032991	cellular_component	protein-containing complex
D	0042802	molecular_function	identical protein binding
D	0051289	biological_process	protein homotetramerization
D	0070404	molecular_function	NADH binding
D	1902494	cellular_component	catalytic complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAD A 501

Chain	Residue
A	GLY13
A	VAL65
A	SER91
A	ILE92
A	GLY93
A	LEU144
A	SER145
A	LYS163
A	ALA189
A	GLY190
A	PRO191
A	VAL14
A	ILE192
A	THR194
A	ALA196
A	TCL601
A	HOH608
A	HOH611
A	HOH617
A	HOH619
A	HOH649
A	HOH662
A	ALA15
A	HOH667
A	SER19
A	ILE20
A	GLN40
A	LEU44
A	CYS63
A	ASP64

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TCL A 601

Chain	Residue
A	GLY93
A	ALA95
A	LEU100
A	TYR146
A	TYR156
A	ALA196
A	ILE200
A	NAD501

site_id	AC3
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAD B 502

Chain	Residue
B	GLY13
B	VAL14
B	ALA15
B	SER19
B	ILE20
B	GLN40
B	LEU44
B	CYS63
B	ASP64
B	VAL65
B	SER91
B	ILE92
B	GLY93
B	LEU144
B	SER145
B	LYS163
B	ALA189
B	GLY190
B	PRO191
B	ILE192
B	THR194
B	ALA196
B	TCL602
B	HOH612
B	HOH615
B	HOH621
B	HOH623
B	HOH653
B	HOH666
B	HOH671

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TCL B 602

Chain	Residue
B	GLY93
B	ALA95
B	LEU100
B	TYR146
B	TYR156
B	ALA196
B	ILE200
B	NAD502

site_id	AC5
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAD C 503

Chain	Residue
C	HOH614
C	HOH617
C	HOH623
C	HOH625
C	HOH655
C	HOH668
C	HOH673
C	GLY13
C	VAL14
C	ALA15
C	SER19
C	ILE20
C	GLN40
C	LEU44
C	CYS63
C	ASP64
C	VAL65
C	SER91
C	ILE92
C	GLY93
C	LEU144
C	SER145
C	LYS163
C	ALA189
C	GLY190
C	PRO191
C	ILE192
C	THR194
C	ALA196
C	TCL603

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TCL C 603

Chain	Residue
C	GLY93
C	ALA95
C	LEU100
C	TYR146
C	TYR156
C	ALA196
C	ILE200
C	NAD503

site_id	AC7
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAD D 504

Chain	Residue
D	GLY13
D	VAL14
D	ALA15
D	SER19
D	ILE20
D	GLN40
D	LEU44
D	CYS63
D	ASP64
D	VAL65
D	SER91
D	ILE92
D	GLY93
D	LEU144
D	SER145
D	LYS163
D	ALA189
D	GLY190
D	PRO191
D	ILE192
D	THR194
D	ALA196
D	TCL604
D	HOH618
D	HOH621
D	HOH627
D	HOH629
D	HOH659
D	HOH672
D	HOH677

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TCL D 604

Chain	Residue
D	GLY93
D	ALA95
D	LEU100
D	TYR146
D	TYR156
D	ALA196
D	ILE200
D	NAD504

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10201369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10398587","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10493822","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10595560","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11514139","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12109908","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12699381","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8953047","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Site: {"description":"Involved in acyl-ACP binding"}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	GLU150

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

Chain	Residue	Details
A	TYR156
A	LYS163

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
B	TYR156
B	LYS163

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
C	TYR156
C	LYS163

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
D	TYR156
D	LYS163

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
A	MET159
A	LYS163

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
B	MET159
B	LYS163

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
C	MET159
C	LYS163

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
D	MET159
D	LYS163

site_id	MCSA1
Number of Residues	2
Details	M-CSA 606

Chain	Residue	Details
A	TYR156	proton acceptor, proton donor
A	LYS163	electrostatic stabiliser

site_id	MCSA2
Number of Residues	2
Details	M-CSA 606

Chain	Residue	Details
B	TYR156	proton acceptor, proton donor
B	LYS163	electrostatic stabiliser

site_id	MCSA3
Number of Residues	2
Details	M-CSA 606

Chain	Residue	Details
C	TYR156	proton acceptor, proton donor
C	LYS163	electrostatic stabiliser

site_id	MCSA4
Number of Residues	2
Details	M-CSA 606

Chain	Residue	Details
D	TYR156	proton acceptor, proton donor
D	LYS163	electrostatic stabiliser

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