3PWI

Crystal structure of the mutant P34A of D-Glucarate dehydratase from Escherichia coli complexed with product 5-keto-4-deoxy-D-Glucarate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0008872	molecular_function	glucarate dehydratase activity
A	0042838	biological_process	D-glucarate catabolic process
B	0000287	molecular_function	magnesium ion binding
B	0008872	molecular_function	glucarate dehydratase activity
B	0042838	biological_process	D-glucarate catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 447

Chain	Residue
A	ASP235
A	ASN237
A	GLU260
A	ASP261
A	ASN289
A	GLR448

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 447

Chain	Residue
B	ASP261
B	ASN289
B	GLR448
B	ASP235
B	ASN237
B	GLU260

---

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE GLR A 448

Chain	Residue
A	ASN27
A	HIS32
A	THR103
A	TYR150
A	LYS205
A	LYS207
A	ASP235
A	ASN237
A	GLU260
A	ASN289
A	HIS339
A	SER340
A	ASN341
A	HIS368
A	ARG422
A	MG447
A	HOH492

---

site_id	AC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE GLR B 448

Chain	Residue
B	ASN27
B	HIS32
B	THR103
B	TYR150
B	LYS205
B	LYS207
B	ASP235
B	ASN237
B	GLU260
B	ASN289
B	HIS339
B	SER340
B	ASN341
B	HIS368
B	ARG422
B	MG447
B	HOH455
B	HOH464

---

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL B 449

Chain	Residue
A	ARG280
B	GLY299
B	LEU302
B	SER303
B	PHE332
B	HOH523
B	HOH523
B	HOH535
B	HOH544

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 449

Chain	Residue
A	GLY299
A	LEU302
A	SER303
A	GLN305
A	PHE332
A	HOH467
A	HOH485
A	HOH485
B	ARG280

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11513584","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11513584","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JCT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10769114","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11513584","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of the mutant of D-Glucarate dehydratase from Escherichia Coli complexed with product 5-keto-4-deoxy-D-Glucarate.","authors":["Fedorov A.A.","Fedorov E.V.","Lukk T.","Gerlt J.A.","Almo S.C."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2012","submissionDatabase":"PDB data bank","title":"Glucarate dehydratase and its related protein from Escherichia coli form a heterotetrameric complex.","authors":["Lukk T.","Ghasempur S.","Imker H.J.","Nair S.K.","Gerlt J.A."]}},{"source":"PDB","id":"1EC7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EC8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EC9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ECQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JCT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JDF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PWG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PWI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4GYP","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10769114","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11513584","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of the mutant of D-Glucarate dehydratase from Escherichia Coli complexed with product 5-keto-4-deoxy-D-Glucarate.","authors":["Fedorov A.A.","Fedorov E.V.","Lukk T.","Gerlt J.A.","Almo S.C."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2012","submissionDatabase":"PDB data bank","title":"Glucarate dehydratase and its related protein from Escherichia coli form a heterotetrameric complex.","authors":["Lukk T.","Ghasempur S.","Imker H.J.","Nair S.K.","Gerlt J.A."]}},{"source":"PDB","id":"1EC7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EC8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JDF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PWG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PWI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4GYP","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	9
Details	M-CSA 451

Chain	Residue	Details
A	LYS205	electrostatic stabiliser
A	LYS207	electrostatic stabiliser
A	ASP235	metal ligand
A	ASN237	activator, electrostatic stabiliser
A	GLU260	metal ligand
A	ASN289	metal ligand
A	ASP313	electrostatic stabiliser, modifies pKa
A	HIS339	proton acceptor, proton donor
A	ASN341	activator

---

site_id	MCSA2
Number of Residues	9
Details	M-CSA 451

Chain	Residue	Details
B	LYS205	electrostatic stabiliser
B	LYS207	electrostatic stabiliser
B	ASP235	metal ligand
B	ASN237	activator, electrostatic stabiliser
B	GLU260	metal ligand
B	ASN289	metal ligand
B	ASP313	electrostatic stabiliser, modifies pKa
B	HIS339	proton acceptor, proton donor
B	ASN341	activator

---