Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4ELX

Structure of apo E.coli. 1,4-dihydroxy-2- naphthoyl CoA synthases with Cl

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0008935	molecular_function	1,4-dihydroxy-2-naphthoyl-CoA synthase activity
A	0009234	biological_process	menaquinone biosynthetic process
A	0016829	molecular_function	lyase activity
A	0071890	molecular_function	bicarbonate binding
B	0003824	molecular_function	catalytic activity
B	0005515	molecular_function	protein binding
B	0005829	cellular_component	cytosol
B	0008935	molecular_function	1,4-dihydroxy-2-naphthoyl-CoA synthase activity
B	0009234	biological_process	menaquinone biosynthetic process
B	0016829	molecular_function	lyase activity
B	0071890	molecular_function	bicarbonate binding
C	0003824	molecular_function	catalytic activity
C	0005515	molecular_function	protein binding
C	0005829	cellular_component	cytosol
C	0008935	molecular_function	1,4-dihydroxy-2-naphthoyl-CoA synthase activity
C	0009234	biological_process	menaquinone biosynthetic process
C	0016829	molecular_function	lyase activity
C	0071890	molecular_function	bicarbonate binding
D	0003824	molecular_function	catalytic activity
D	0005515	molecular_function	protein binding
D	0005829	cellular_component	cytosol
D	0008935	molecular_function	1,4-dihydroxy-2-naphthoyl-CoA synthase activity
D	0009234	biological_process	menaquinone biosynthetic process
D	0016829	molecular_function	lyase activity
D	0071890	molecular_function	bicarbonate binding
E	0003824	molecular_function	catalytic activity
E	0005515	molecular_function	protein binding
E	0005829	cellular_component	cytosol
E	0008935	molecular_function	1,4-dihydroxy-2-naphthoyl-CoA synthase activity
E	0009234	biological_process	menaquinone biosynthetic process
E	0016829	molecular_function	lyase activity
E	0071890	molecular_function	bicarbonate binding
F	0003824	molecular_function	catalytic activity
F	0005515	molecular_function	protein binding
F	0005829	cellular_component	cytosol
F	0008935	molecular_function	1,4-dihydroxy-2-naphthoyl-CoA synthase activity
F	0009234	biological_process	menaquinone biosynthetic process
F	0016829	molecular_function	lyase activity
F	0071890	molecular_function	bicarbonate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 301

Chain	Residue
A	THR203
A	VAL205
A	GLU213
A	ARG216
A	TRP217
C	ARG188

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL A 302

Chain	Residue
A	GLY156
A	TRP184
A	HOH536
A	GLY132
A	GLN154
A	THR155

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 301

Chain	Residue
B	GLU213
B	ARG216
B	TRP217
E	ARG188

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL B 302

Chain	Residue
B	GLY132
B	GLN154
B	THR155
B	GLY156
B	TRP184

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PEG B 303

Chain	Residue
B	ARG173
B	ILE174
B	VAL175
B	GLY176
B	HOH419
B	HOH502
E	GLY176
F	ILE174
F	VAL175
F	GLY176

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 301

Chain	Residue
C	THR203
C	VAL205
C	GLU213
C	ARG216
C	TRP217
D	ARG188

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CL C 302

Chain	Residue
C	GLY132
C	GLN154
C	THR155
C	GLY156
C	TRP184
C	HOH477
C	HOH482

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PEG C 303

Chain	Residue
A	ARG173
A	ILE174
A	VAL175
A	GLY176
C	ALA172
C	ARG173
C	HOH407
D	ALA172
D	VAL175

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 C 304

Chain	Residue
C	THR75
C	GLY76
C	GLY78
C	ASP79
C	MET125
C	GLU211
C	HOH483

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 301

Chain	Residue
A	ARG188
D	THR203
D	VAL205
D	GLU213
D	ARG216
D	TRP217

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CL D 302

Chain	Residue
D	GLY132
D	GLN154
D	THR155
D	GLY156
D	TRP184
D	HOH484
D	HOH485

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PEG D 303

Chain	Residue
B	GLN243
C	ALA238
C	ASP239
C	HOH467
D	ARG173
D	ASP239
D	CYS240
D	HOH404
D	HOH417

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL E 301

Chain	Residue
E	TYR10
E	THR203
E	VAL205
E	GLU213
E	ARG216
E	TRP217
E	HOH487
F	ARG188

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO E 302

Chain	Residue
B	HOH519
C	GLN247
E	GLY165
E	TRP166
E	GLY167
E	ALA168
E	SER169

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL F 301

Chain	Residue
F	VAL205
F	GLU213
F	TRP217
B	ARG188
F	THR203

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL F 302

Chain	Residue
F	GLY132
F	GLN154
F	THR155
F	GLY156
F	TRP184

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL F 303

Chain	Residue
B	HOH529
F	ARG173
F	ASP239
F	HOH430

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL F 304

Chain	Residue
F	THR75
F	GLY76
F	GLY78
F	ASP79
F	HOH414
F	HOH466

Functional Information from PROSITE/UniProt

site_id	PS00166
Number of Residues	21
Details	ENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. VAmVAGysiGGGhvlhMmCDL

Chain	Residue	Details
A	VAL123-LEU143

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21830810","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23658663","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	10
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"21830810","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23658663","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22606952","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23658663","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21830810","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21830810","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23658663","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Site: {"description":"Important for catalysis","evidences":[{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21830810","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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