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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3ES8

Crystal structure of divergent enolase from Oceanobacillus Iheyensis complexed with Mg and L-malate.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016829	molecular_function	lyase activity
A	0046872	molecular_function	metal ion binding
B	0016829	molecular_function	lyase activity
B	0046872	molecular_function	metal ion binding
C	0016829	molecular_function	lyase activity
C	0046872	molecular_function	metal ion binding
D	0016829	molecular_function	lyase activity
D	0046872	molecular_function	metal ion binding
E	0016829	molecular_function	lyase activity
E	0046872	molecular_function	metal ion binding
F	0016829	molecular_function	lyase activity
F	0046872	molecular_function	metal ion binding
G	0016829	molecular_function	lyase activity
G	0046872	molecular_function	metal ion binding
H	0016829	molecular_function	lyase activity
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE LMR A 392

Chain	Residue
A	ARG15
A	MG393
A	HOH468
A	HOH472
A	ASP42
A	HIS45
A	TYR89
A	TYR90
A	TYR164
A	THR297
A	GLN298
A	ARG385

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 393

Chain	Residue
A	ASP42
A	HIS45
A	THR297
A	LMR392

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE LMR B 392

Chain	Residue
B	ARG15
B	ASP42
B	HIS45
B	TYR89
B	TYR90
B	TYR164
B	THR297
B	GLN298
B	ARG385
B	MG393
B	HOH439
B	HOH443

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 393

Chain	Residue
B	ASP42
B	HIS45
B	THR297
B	LMR392

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE LMR C 392

Chain	Residue
C	ARG15
C	ASP42
C	HIS45
C	TYR89
C	TYR90
C	PHE135
C	TYR164
C	THR297
C	GLN298
C	ARG385
C	MG393

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 393

Chain	Residue
C	ASP42
C	HIS45
C	THR297
C	LMR392

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE LMR D 392

Chain	Residue
D	ARG15
D	ASP42
D	HIS45
D	TYR89
D	TYR90
D	TYR164
D	THR297
D	GLN298
D	ARG385
D	MG393
D	HOH452
D	HOH454

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 393

Chain	Residue
D	ASP42
D	HIS45
D	THR297
D	LMR392

site_id	AC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE LMR E 392

Chain	Residue
E	ARG15
E	ASP42
E	HIS45
E	TYR89
E	TYR90
E	TYR164
E	THR297
E	GLN298
E	ARG385
E	MG393
E	HOH457
E	HOH460

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG E 393

Chain	Residue
E	ASP42
E	HIS45
E	THR297
E	LMR392

site_id	BC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE LMR F 392

Chain	Residue
F	ARG15
F	ASP42
F	HIS45
F	TYR89
F	TYR90
F	TYR164
F	THR297
F	GLN298
F	ARG385
F	MG393
F	HOH464

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG F 393

Chain	Residue
F	ASP42
F	HIS45
F	THR297
F	LMR392

site_id	BC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE LMR G 392

Chain	Residue
G	TYR164
G	THR297
G	GLN298
G	ARG385
G	MG393
G	HOH431
G	HOH455
G	HOH456
G	ARG15
G	ASP42
G	HIS45
G	TYR89
G	TYR90

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG G 393

Chain	Residue
G	ASP42
G	HIS45
G	THR297
G	LMR392

site_id	BC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE LMR H 392

Chain	Residue
H	ARG15
H	ASP42
H	HIS45
H	TYR89
H	TYR90
H	PHE135
H	TYR164
H	THR297
H	GLN298
H	ARG385
H	MG393
H	HOH442
H	HOH445

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG H 393

Chain	Residue
H	ASP42
H	HIS45
H	THR297
H	LMR392

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"19883118","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"19883118","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	80
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Site: {"description":"Increases basicity of active site Tyr"}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	9
Details	M-CSA 502

Chain	Residue	Details
A	ASP42	metal ligand
A	HIS45	metal ligand
A	TYR90	proton acceptor, proton donor
A	ARG162	electrostatic stabiliser, modifies pKa
A	TYR164	proton acceptor, proton donor
A	ASP193	metal ligand
A	GLU221	metal ligand
A	HIS246	metal ligand
A	THR297	metal ligand

site_id	MCSA2
Number of Residues	9
Details	M-CSA 502

Chain	Residue	Details
B	ASP42	metal ligand
B	HIS45	metal ligand
B	TYR90	proton acceptor, proton donor
B	ARG162	electrostatic stabiliser, modifies pKa
B	TYR164	proton acceptor, proton donor
B	ASP193	metal ligand
B	GLU221	metal ligand
B	HIS246	metal ligand
B	THR297	metal ligand

site_id	MCSA3
Number of Residues	9
Details	M-CSA 502

Chain	Residue	Details
C	ASP42	metal ligand
C	HIS45	metal ligand
C	TYR90	proton acceptor, proton donor
C	ARG162	electrostatic stabiliser, modifies pKa
C	TYR164	proton acceptor, proton donor
C	ASP193	metal ligand
C	GLU221	metal ligand
C	HIS246	metal ligand
C	THR297	metal ligand

site_id	MCSA4
Number of Residues	9
Details	M-CSA 502

Chain	Residue	Details
D	ASP42	metal ligand
D	HIS45	metal ligand
D	TYR90	proton acceptor, proton donor
D	ARG162	electrostatic stabiliser, modifies pKa
D	TYR164	proton acceptor, proton donor
D	ASP193	metal ligand
D	GLU221	metal ligand
D	HIS246	metal ligand
D	THR297	metal ligand

site_id	MCSA5
Number of Residues	9
Details	M-CSA 502

Chain	Residue	Details
E	ASP42	metal ligand
E	HIS45	metal ligand
E	TYR90	proton acceptor, proton donor
E	ARG162	electrostatic stabiliser, modifies pKa
E	TYR164	proton acceptor, proton donor
E	ASP193	metal ligand
E	GLU221	metal ligand
E	HIS246	metal ligand
E	THR297	metal ligand

site_id	MCSA6
Number of Residues	9
Details	M-CSA 502

Chain	Residue	Details
F	ASP42	metal ligand
F	HIS45	metal ligand
F	TYR90	proton acceptor, proton donor
F	ARG162	electrostatic stabiliser, modifies pKa
F	TYR164	proton acceptor, proton donor
F	ASP193	metal ligand
F	GLU221	metal ligand
F	HIS246	metal ligand
F	THR297	metal ligand

site_id	MCSA7
Number of Residues	9
Details	M-CSA 502

Chain	Residue	Details
G	ASP42	metal ligand
G	HIS45	metal ligand
G	TYR90	proton acceptor, proton donor
G	ARG162	electrostatic stabiliser, modifies pKa
G	TYR164	proton acceptor, proton donor
G	ASP193	metal ligand
G	GLU221	metal ligand
G	HIS246	metal ligand
G	THR297	metal ligand

site_id	MCSA8
Number of Residues	9
Details	M-CSA 502

Chain	Residue	Details
H	ASP42	metal ligand
H	HIS45	metal ligand
H	TYR90	proton acceptor, proton donor
H	ARG162	electrostatic stabiliser, modifies pKa
H	TYR164	proton acceptor, proton donor
H	ASP193	metal ligand
H	GLU221	metal ligand
H	HIS246	metal ligand
H	THR297	metal ligand

239803

PDB entries from 2025-08-06

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