Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4ELS

Structure of E. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme A synthases (MENB) in complex with bicarbonate

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	7
Details	BINDING SITE FOR RESIDUE BCT A 301

Chain	Residue
A	GLY132
A	GLY133
A	GLN154
A	THR155
A	GLY156
A	SER161
A	PHE162

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 302

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

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO A 303

Chain	Residue
A	CL304
D	ILE174

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 304

Chain	Residue
A	EDO303
C	HOH452

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 305

Chain	Residue
A	ARG173
A	ASP239
A	CYS240
A	HOH419
D	ALA238
D	ASP239

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BCT B 301

Chain	Residue
B	GLY132
B	GLY133
B	GLN154
B	THR155
B	GLY156
B	SER161
B	TRP184
B	HOH472

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BCT B 302

Chain	Residue
B	GLU213
B	TRP217
E	ARG188

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 304

Chain	Residue
B	PHE22
B	GLU23
B	ILE25
B	ARG26
B	ASN40

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BCT C 301

Chain	Residue
C	GLY132
C	GLY133
C	GLN154
C	THR155
C	GLY156
C	SER161
C	PHE162
C	TRP184

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 302

Chain	Residue
C	THR203
C	VAL205
C	GLU213
C	ARG216
C	TRP217
C	HOH455
D	ARG188

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BCT D 301

Chain	Residue
D	GLY132
D	GLY133
D	GLN154
D	THR155
D	GLY156
D	SER161
D	TRP184
D	HOH435
D	HOH459

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BCT D 302

Chain	Residue
A	ARG188
D	GLU213
D	TRP217

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL D 303

Chain	Residue
C	HOH401
D	ARG173
D	ASP239
D	CYS240

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BCT E 301

Chain	Residue
E	GLY132
E	GLY133
E	GLN154
E	THR155
E	GLY156
E	SER161
E	HOH461

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BCT E 302

Chain	Residue
E	THR203
E	GLU213
E	TRP217
E	HOH421
F	ARG188

site_id	BC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE BCT F 301

Chain	Residue
F	GLY132
F	GLY133
F	GLN154
F	THR155
F	GLY156
F	SER161
F	PHE162
F	ASP163
F	TRP184
F	HOH456

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL F 302

Chain	Residue
B	ARG188
F	THR203
F	VAL205
F	GLU213
F	ARG216
F	TRP217
F	HOH431

site_id	BC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PEG F 303

Chain	Residue
E	HOH435

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO F 304

Chain	Residue
A	TYR258
F	HOH442
F	HOH456

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	18
Details	BINDING: in other chain => ECO:0000255\|HAMAP-Rule:MF_01934, ECO:0000269\|PubMed:21830810, ECO:0000269\|PubMed:23658663

Chain	Residue	Details
A	ARG45
D	ARG45
D	TYR129
D	THR155
E	ARG45
E	TYR129
E	THR155
F	ARG45
F	TYR129
F	THR155
A	TYR129
A	THR155
B	ARG45
B	TYR129
B	THR155
C	ARG45
C	TYR129
C	THR155

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: in other chain => ECO:0000269\|PubMed:21830810, ECO:0000269\|PubMed:23658663

Chain	Residue	Details
A	SER84
B	SER84
C	SER84
D	SER84
E	SER84
F	SER84

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: in other chain => ECO:0000255\|HAMAP-Rule:MF_01934, ECO:0000269\|PubMed:21830810

Chain	Residue	Details
A	TYR97
B	TYR97
C	TYR97
D	TYR97
E	TYR97
F	TYR97

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01934, ECO:0000269\|PubMed:22606952

Chain	Residue	Details
A	GLN154
B	GLN154
C	GLN154
D	GLN154
E	GLN154
F	GLN154

site_id	SWS_FT_FI5
Number of Residues	6
Details	BINDING: in other chain => ECO:0000255\|HAMAP-Rule:MF_01934, ECO:0000269\|PubMed:23658663

Chain	Residue	Details
A	SER161
B	SER161
C	SER161
D	SER161
E	SER161
F	SER161

site_id	SWS_FT_FI6
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01934, ECO:0000269\|PubMed:21830810

Chain	Residue	Details
A	TYR258
B	TYR258
C	TYR258
D	TYR258
E	TYR258
F	TYR258

site_id	SWS_FT_FI7
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01934, ECO:0000269\|PubMed:21830810, ECO:0000269\|PubMed:23658663

Chain	Residue	Details
A	LYS273
B	LYS273
C	LYS273
D	LYS273
E	LYS273
F	LYS273

site_id	SWS_FT_FI8
Number of Residues	12
Details	SITE: Important for catalysis => ECO:0000255\|HAMAP-Rule:MF_01934, ECO:0000305\|PubMed:21830810

Chain	Residue	Details
A	TYR97
E	TYR258
F	TYR97
F	TYR258
A	TYR258
B	TYR97
B	TYR258
C	TYR97
C	TYR258
D	TYR97
D	TYR258
E	TYR97

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