Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8W21

Crystal Structure of Enolase from Chlamydia trachomatis (P43212 Form)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000015	cellular_component	phosphopyruvate hydratase complex
A	0000287	molecular_function	magnesium ion binding
A	0004634	molecular_function	phosphopyruvate hydratase activity
A	0005576	cellular_component	extracellular region
A	0005737	cellular_component	cytoplasm
A	0006096	biological_process	glycolytic process
A	0009986	cellular_component	cell surface
A	0016829	molecular_function	lyase activity
A	0046872	molecular_function	metal ion binding
B	0000015	cellular_component	phosphopyruvate hydratase complex
B	0000287	molecular_function	magnesium ion binding
B	0004634	molecular_function	phosphopyruvate hydratase activity
B	0005576	cellular_component	extracellular region
B	0005737	cellular_component	cytoplasm
B	0006096	biological_process	glycolytic process
B	0009986	cellular_component	cell surface
B	0016829	molecular_function	lyase activity
B	0046872	molecular_function	metal ion binding
C	0000015	cellular_component	phosphopyruvate hydratase complex
C	0000287	molecular_function	magnesium ion binding
C	0004634	molecular_function	phosphopyruvate hydratase activity
C	0005576	cellular_component	extracellular region
C	0005737	cellular_component	cytoplasm
C	0006096	biological_process	glycolytic process
C	0009986	cellular_component	cell surface
C	0016829	molecular_function	lyase activity
C	0046872	molecular_function	metal ion binding
D	0000015	cellular_component	phosphopyruvate hydratase complex
D	0000287	molecular_function	magnesium ion binding
D	0004634	molecular_function	phosphopyruvate hydratase activity
D	0005576	cellular_component	extracellular region
D	0005737	cellular_component	cytoplasm
D	0006096	biological_process	glycolytic process
D	0009986	cellular_component	cell surface
D	0016829	molecular_function	lyase activity
D	0046872	molecular_function	metal ion binding
E	0000015	cellular_component	phosphopyruvate hydratase complex
E	0000287	molecular_function	magnesium ion binding
E	0004634	molecular_function	phosphopyruvate hydratase activity
E	0005576	cellular_component	extracellular region
E	0005737	cellular_component	cytoplasm
E	0006096	biological_process	glycolytic process
E	0009986	cellular_component	cell surface
E	0016829	molecular_function	lyase activity
E	0046872	molecular_function	metal ion binding
F	0000015	cellular_component	phosphopyruvate hydratase complex
F	0000287	molecular_function	magnesium ion binding
F	0004634	molecular_function	phosphopyruvate hydratase activity
F	0005576	cellular_component	extracellular region
F	0005737	cellular_component	cytoplasm
F	0006096	biological_process	glycolytic process
F	0009986	cellular_component	cell surface
F	0016829	molecular_function	lyase activity
F	0046872	molecular_function	metal ion binding
G	0000015	cellular_component	phosphopyruvate hydratase complex
G	0000287	molecular_function	magnesium ion binding
G	0004634	molecular_function	phosphopyruvate hydratase activity
G	0005576	cellular_component	extracellular region
G	0005737	cellular_component	cytoplasm
G	0006096	biological_process	glycolytic process
G	0009986	cellular_component	cell surface
G	0016829	molecular_function	lyase activity
G	0046872	molecular_function	metal ion binding
H	0000015	cellular_component	phosphopyruvate hydratase complex
H	0000287	molecular_function	magnesium ion binding
H	0004634	molecular_function	phosphopyruvate hydratase activity
H	0005576	cellular_component	extracellular region
H	0005737	cellular_component	cytoplasm
H	0006096	biological_process	glycolytic process
H	0009986	cellular_component	cell surface
H	0016829	molecular_function	lyase activity
H	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00164
Number of Residues	14
Details	ENOLASE Enolase signature. VLIKpNQIGTLTET

Chain	Residue	Details
A	VAL332-THR345

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton donor => ECO:0000255\|HAMAP-Rule:MF_00318

Chain	Residue	Details
A	GLU207
B	GLU207
C	GLU207
D	GLU207
E	GLU207
F	GLU207
G	GLU207
H	GLU207

site_id	SWS_FT_FI2
Number of Residues	8
Details	ACT_SITE: Proton acceptor => ECO:0000255\|HAMAP-Rule:MF_00318

Chain	Residue	Details
A	LYS335
B	LYS335
C	LYS335
D	LYS335
E	LYS335
F	LYS335
G	LYS335
H	LYS335

site_id	SWS_FT_FI3
Number of Residues	56
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00318

Chain	Residue	Details
A	HIS157
B	ASP244
B	GLU283
B	ASP310
B	SER362
B	LYS386
C	HIS157
C	GLU166
C	ASP244
C	GLU283
C	ASP310
A	GLU166
C	SER362
C	LYS386
D	HIS157
D	GLU166
D	ASP244
D	GLU283
D	ASP310
D	SER362
D	LYS386
E	HIS157
A	ASP244
E	GLU166
E	ASP244
E	GLU283
E	ASP310
E	SER362
E	LYS386
F	HIS157
F	GLU166
F	ASP244
F	GLU283
A	GLU283
F	ASP310
F	SER362
F	LYS386
G	HIS157
G	GLU166
G	ASP244
G	GLU283
G	ASP310
G	SER362
G	LYS386
A	ASP310
H	HIS157
H	GLU166
H	ASP244
H	GLU283
H	ASP310
H	SER362
H	LYS386
A	SER362
A	LYS386
B	HIS157
B	GLU166

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: covalent; in inhibited form => ECO:0000255\|HAMAP-Rule:MF_00318

Chain	Residue	Details
A	LYS335
B	LYS335
C	LYS335
D	LYS335
E	LYS335
F	LYS335
G	LYS335
H	LYS335

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