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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2OQY

The crystal structure of muconate cycloisomerase from Oceanobacillus iheyensis

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	6
Details	BINDING SITE FOR RESIDUE MG A 401

Chain	Residue
A	ASP193
A	GLU221
A	HIS246
A	HOH479
A	HOH480
A	HOH481

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 402

Chain	Residue
A	ASP42
A	HIS45
A	THR297

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 401

Chain	Residue
B	ASP193
B	GLU221
B	HIS246
B	HOH475
B	HOH476
B	HOH477

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 402

Chain	Residue
B	ASP42
B	HIS45
B	THR297
B	HOH470

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 401

Chain	Residue
C	ASP193
C	GLU221
C	HIS246
C	HOH472
C	HOH473
C	HOH474

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 402

Chain	Residue
C	ASP42
C	HIS45
C	THR297

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 401

Chain	Residue
D	ASP193
D	GLU221
D	HIS246
D	HOH478
D	HOH479
D	HOH480

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG D 402

Chain	Residue
D	ASP42
D	HIS45
D	THR297

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG E 401

Chain	Residue
E	ASP193
E	GLU221
E	HIS246
E	HOH481
E	HOH482
E	HOH483

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG E 402

Chain	Residue
E	ASP42
E	HIS45
E	THR297

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG F 401

Chain	Residue
F	ASP193
F	GLU221
F	HIS246
F	HOH478
F	HOH479
F	HOH480

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG F 402

Chain	Residue
F	ASP42
F	HIS45
F	THR297

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG G 401

Chain	Residue
G	ASP193
G	GLU221
G	HIS246
G	HOH480
G	HOH481
G	HOH482

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG G 402

Chain	Residue
G	ASP42
G	HIS45
G	THR297

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG H 401

Chain	Residue
H	ASP193
H	GLU221
H	HIS246
H	HOH483
H	HOH484
H	HOH485

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG H 402

Chain	Residue
H	ASP42
H	HIS45
H	THR297

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	72
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

245663

PDB entries from 2025-12-03

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