3TWA

Crystal structure of gluconate dehydratase (TARGET EFI-501679) from Salmonella enterica subsp. enterica serovar Enteritidis str. P125109 complexed with magnesium and glycerol

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0009063	biological_process	amino acid catabolic process
A	0016052	biological_process	carbohydrate catabolic process
A	0016829	molecular_function	lyase activity
A	0046872	molecular_function	metal ion binding
A	0047929	molecular_function	gluconate dehydratase activity
B	0000287	molecular_function	magnesium ion binding
B	0009063	biological_process	amino acid catabolic process
B	0016052	biological_process	carbohydrate catabolic process
B	0016829	molecular_function	lyase activity
B	0046872	molecular_function	metal ion binding
B	0047929	molecular_function	gluconate dehydratase activity
C	0000287	molecular_function	magnesium ion binding
C	0009063	biological_process	amino acid catabolic process
C	0016052	biological_process	carbohydrate catabolic process
C	0016829	molecular_function	lyase activity
C	0046872	molecular_function	metal ion binding
C	0047929	molecular_function	gluconate dehydratase activity
D	0000287	molecular_function	magnesium ion binding
D	0009063	biological_process	amino acid catabolic process
D	0016052	biological_process	carbohydrate catabolic process
D	0016829	molecular_function	lyase activity
D	0046872	molecular_function	metal ion binding
D	0047929	molecular_function	gluconate dehydratase activity
E	0000287	molecular_function	magnesium ion binding
E	0009063	biological_process	amino acid catabolic process
E	0016052	biological_process	carbohydrate catabolic process
E	0016829	molecular_function	lyase activity
E	0046872	molecular_function	metal ion binding
E	0047929	molecular_function	gluconate dehydratase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 420

Chain	Residue
A	ASP225
A	GLU251
A	GLU277
A	HOH424
A	HOH518
A	HOH708

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 421

Chain	Residue
A	GLU277
A	HIS327
A	PRO329
A	ASP331
A	HOH492
B	TYR82
B	TRP83
A	GLN45
A	TYR160
A	HIS227

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 422

Chain	Residue
A	GLY330
A	ILE332
A	PRO334
A	VAL337
A	THR356
A	PRO357
A	MET358
A	LEU362
A	HOH482
A	HOH536

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 423

Chain	Residue
A	GLY86
A	ILE88
B	PRO87
B	ILE88

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 420

Chain	Residue
B	ASP225
B	GLU251
B	GLU277
B	HOH423
B	HOH517
B	HOH622

---

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL B 421

Chain	Residue
A	TYR82
A	TRP83
B	GLN45
B	TYR160
B	HIS227
B	GLU277
B	HIS327
B	PRO329
B	ASP331
B	HOH538

---

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL B 422

Chain	Residue
B	GLY330
B	ILE332
B	PRO334
B	VAL337
B	THR356
B	PRO357
B	MET358
B	LEU362
B	HOH490
B	HOH509

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 420

Chain	Residue
C	ASP225
C	GLU251
C	GLU277
C	HOH431
C	HOH520
C	HOH675

---

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL C 421

Chain	Residue
C	GLN45
C	TYR160
C	HIS227
C	GLU277
C	HIS327
C	PRO329
C	ASP331
C	HOH566
D	TYR82
D	TRP83

---

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL C 422

Chain	Residue
C	GLY330
C	ILE332
C	PRO334
C	VAL337
C	THR356
C	PRO357
C	LEU362
C	HOH505
C	HOH536

---

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL C 423

Chain	Residue
C	GLY86
C	PRO87
C	ILE88
D	PRO87
D	ILE88

---

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 420

Chain	Residue
D	ASP225
D	GLU251
D	GLU277
D	HOH528
D	HOH580
D	HOH618

---

site_id	BC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL D 421

Chain	Residue
D	PRO329
D	ASP331
D	HOH497
C	TYR82
C	TRP83
D	GLN45
D	TYR160
D	HIS227
D	GLU277
D	HIS327

---

site_id	BC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL D 422

Chain	Residue
D	ILE332
D	PRO334
D	VAL337
D	THR356
D	PRO357
D	MET358
D	LEU362
D	HOH501
D	HOH504

---

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL E 420

Chain	Residue
E	GLN45
E	TRP83
E	TYR160
E	HIS227
E	HIS327
E	PRO329
E	ASP331

---

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG E 421

Chain	Residue
E	ASP225
E	GLU251
E	GLU277
E	HOH422
E	HOH761
E	HOH889

---

Functional Information from PROSITE/UniProt

site_id	PS00908
Number of Residues	26
Details	MR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AlSGVDmALwDIkGKlagmPVydLLG

Chain	Residue	Details
A	ALA92-GLY117

---

site_id	PS00909
Number of Residues	32
Details	MR_MLE_2 Mandelate racemase / muconate lactonizing enzyme family signature 2. FihDvHervtpvtAinlaktLeqyqlfyLEDP

Chain	Residue	Details
A	PHE222-PRO253

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	30
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	5
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24697546","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	5
Details	Site: {"description":"Important for activity and substrate specificity; Pro is observed in family members with low D-mannonate dehydratase activity","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---