Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7E51

Structure of PEP bound Enolase from Mycobacterium tuberculosis

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	0005886	cellular_component	plasma membrane
A	0006096	biological_process	glycolytic process
A	0009274	cellular_component	peptidoglycan-based cell wall
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	0005886	cellular_component	plasma membrane
B	0006096	biological_process	glycolytic process
B	0009274	cellular_component	peptidoglycan-based cell wall
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	0005886	cellular_component	plasma membrane
C	0006096	biological_process	glycolytic process
C	0009274	cellular_component	peptidoglycan-based cell wall
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	0005886	cellular_component	plasma membrane
D	0006096	biological_process	glycolytic process
D	0009274	cellular_component	peptidoglycan-based cell wall
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	0005886	cellular_component	plasma membrane
E	0006096	biological_process	glycolytic process
E	0009274	cellular_component	peptidoglycan-based cell wall
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	0005886	cellular_component	plasma membrane
F	0006096	biological_process	glycolytic process
F	0009274	cellular_component	peptidoglycan-based cell wall
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	0005886	cellular_component	plasma membrane
G	0006096	biological_process	glycolytic process
G	0009274	cellular_component	peptidoglycan-based cell wall
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	0005886	cellular_component	plasma membrane
H	0006096	biological_process	glycolytic process
H	0009274	cellular_component	peptidoglycan-based cell wall
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. LLVKvNQIGTLTET

Chain	Residue	Details
A	LEU332-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, ECO:0000305\|PubMed:37860976

Chain	Residue	Details
A	GLU204
B	GLU204
C	GLU204
D	GLU204
E	GLU204
F	GLU204
G	GLU204
H	GLU204

site_id	SWS_FT_FI2
Number of Residues	8
Details	ACT_SITE: Proton acceptor => ECO:0000255\|HAMAP-Rule:MF_00318, ECO:0000305\|PubMed:37860976

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	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:37860976, ECO:0007744\|PDB:6L7D, ECO:0007744\|PDB:7CLK, ECO:0007744\|PDB:7CLL

Chain	Residue	Details
A	ALA41
B	ALA41
C	ALA41
D	ALA41
E	ALA41
F	ALA41
G	ALA41
H	ALA41

site_id	SWS_FT_FI4
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:37860976, ECO:0007744\|PDB:7E4F

Chain	Residue	Details
A	SER42
E	GLN162
F	SER42
F	GLN162
G	SER42
G	GLN162
H	SER42
H	GLN162
A	GLN162
B	SER42
B	GLN162
C	SER42
C	GLN162
D	SER42
D	GLN162
E	SER42

site_id	SWS_FT_FI5
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:37860976, ECO:0007744\|PDB:7CLL

Chain	Residue	Details
A	GLU163
E	GLU204
F	GLU163
F	GLU204
G	GLU163
G	GLU204
H	GLU163
H	GLU204
A	GLU204
B	GLU163
B	GLU204
C	GLU163
C	GLU204
D	GLU163
D	GLU204
E	GLU163

site_id	SWS_FT_FI6
Number of Residues	16
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00318, ECO:0000269\|PubMed:37860976, ECO:0007744\|PDB:6L7D, ECO:0007744\|PDB:7CKP, ECO:0007744\|PDB:7CLK, ECO:0007744\|PDB:7CLL, ECO:0007744\|PDB:7DLR, ECO:0007744\|PDB:7E4F

Chain	Residue	Details
A	ASP241
E	ASP310
F	ASP241
F	ASP310
G	ASP241
G	ASP310
H	ASP241
H	ASP310
A	ASP310
B	ASP241
B	ASP310
C	ASP241
C	ASP310
D	ASP241
D	ASP310
E	ASP241

site_id	SWS_FT_FI7
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00318, ECO:0000269\|PubMed:37860976, ECO:0007744\|PDB:7CKP

Chain	Residue	Details
A	GLU283
B	GLU283
C	GLU283
D	GLU283
E	GLU283
F	GLU283
G	GLU283
H	GLU283

site_id	SWS_FT_FI8
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:37860976, ECO:0007744\|PDB:7CLK

Chain	Residue	Details
A	ASP311
B	ASP311
C	ASP311
D	ASP311
E	ASP311
F	ASP311
G	ASP311
H	ASP311

site_id	SWS_FT_FI9
Number of Residues	32
Details	BINDING: BINDING => ECO:0000269\|PubMed:37860976, ECO:0007744\|PDB:7DLR, ECO:0007744\|PDB:7E4F

Chain	Residue	Details
A	LYS335
C	ARG364
C	SER365
C	LYS386
D	LYS335
D	ARG364
D	SER365
D	LYS386
E	LYS335
E	ARG364
E	SER365
A	ARG364
E	LYS386
F	LYS335
F	ARG364
F	SER365
F	LYS386
G	LYS335
G	ARG364
G	SER365
G	LYS386
H	LYS335
A	SER365
H	ARG364
H	SER365
H	LYS386
A	LYS386
B	LYS335
B	ARG364
B	SER365
B	LYS386
C	LYS335

site_id	SWS_FT_FI10
Number of Residues	88
Details	MOD_RES: Glutamate methyl ester (Glu) => ECO:0000305\|PubMed:37385399

Chain	Residue	Details
A	GLU45
A	GLU406
A	GLU407
B	GLU45
B	GLU47
B	GLU50
B	GLU73
B	GLU126
B	GLU195
B	GLU204
B	GLU367
A	GLU47
B	GLU369
B	GLU406
B	GLU407
C	GLU45
C	GLU47
C	GLU50
C	GLU73
C	GLU126
C	GLU195
C	GLU204
A	GLU50
C	GLU367
C	GLU369
C	GLU406
C	GLU407
D	GLU45
D	GLU47
D	GLU50
D	GLU73
D	GLU126
D	GLU195
A	GLU73
D	GLU204
D	GLU367
D	GLU369
D	GLU406
D	GLU407
E	GLU45
E	GLU47
E	GLU50
E	GLU73
E	GLU126
A	GLU126
E	GLU195
E	GLU204
E	GLU367
E	GLU369
E	GLU406
E	GLU407
F	GLU45
F	GLU47
F	GLU50
F	GLU73
A	GLU195
F	GLU126
F	GLU195
F	GLU204
F	GLU367
F	GLU369
F	GLU406
F	GLU407
G	GLU45
G	GLU47
G	GLU50
A	GLU204
G	GLU73
G	GLU126
G	GLU195
G	GLU204
G	GLU367
G	GLU369
G	GLU406
G	GLU407
H	GLU45
H	GLU47
A	GLU367
H	GLU50
H	GLU73
H	GLU126
H	GLU195
H	GLU204
H	GLU367
H	GLU369
H	GLU406
H	GLU407
A	GLU369

site_id	SWS_FT_FI11
Number of Residues	56
Details	MOD_RES: Aspartate methyl ester => ECO:0000305\|PubMed:37385399

Chain	Residue	Details
A	ASP72
B	ASP123
B	ASP203
B	ASP210
B	ASP370
B	ASP375
C	ASP72
C	ASP90
C	ASP123
C	ASP203
C	ASP210
A	ASP90
C	ASP370
C	ASP375
D	ASP72
D	ASP90
D	ASP123
D	ASP203
D	ASP210
D	ASP370
D	ASP375
E	ASP72
A	ASP123
E	ASP90
E	ASP123
E	ASP203
E	ASP210
E	ASP370
E	ASP375
F	ASP72
F	ASP90
F	ASP123
F	ASP203
A	ASP203
F	ASP210
F	ASP370
F	ASP375
G	ASP72
G	ASP90
G	ASP123
G	ASP203
G	ASP210
G	ASP370
G	ASP375
A	ASP210
H	ASP72
H	ASP90
H	ASP123
H	ASP203
H	ASP210
H	ASP370
H	ASP375
A	ASP370
A	ASP375
B	ASP72
B	ASP90

site_id	SWS_FT_FI12
Number of Residues	8
Details	MOD_RES: N6-acetyllysine => ECO:0000305\|PubMed:37385399

Chain	Residue	Details
A	LYS102
B	LYS102
C	LYS102
D	LYS102
E	LYS102
F	LYS102
G	LYS102
H	LYS102

site_id	SWS_FT_FI13
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000305\|PubMed:37385399

Chain	Residue	Details
A	SER198
B	SER198
C	SER198
D	SER198
E	SER198
F	SER198
G	SER198
H	SER198

site_id	SWS_FT_FI14
Number of Residues	16
Details	MOD_RES: Phosphothreonine => ECO:0000305\|PubMed:37385399

Chain	Residue	Details
A	THR199
E	THR341
F	THR199
F	THR341
G	THR199
G	THR341
H	THR199
H	THR341
A	THR341
B	THR199
B	THR341
C	THR199
C	THR341
D	THR199
D	THR341
E	THR199

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)