3BOX

Crystal structure of L-rhamnonate dehydratase from Salmonella typhimurium complexed with Mg

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0006091	biological_process	generation of precursor metabolites and energy
A	0009063	biological_process	amino acid catabolic process
A	0016052	biological_process	carbohydrate catabolic process
A	0016836	molecular_function	hydro-lyase activity
A	0050032	molecular_function	L-rhamnonate dehydratase activity
B	0000287	molecular_function	magnesium ion binding
B	0006091	biological_process	generation of precursor metabolites and energy
B	0009063	biological_process	amino acid catabolic process
B	0016052	biological_process	carbohydrate catabolic process
B	0016836	molecular_function	hydro-lyase activity
B	0050032	molecular_function	L-rhamnonate dehydratase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 501

Chain	Residue
A	ASP226
A	GLU252
A	GLU280
A	HOH539
A	HOH584
A	HOH698

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 501

Chain	Residue
B	HOH583
B	HOH658
B	HOH723
B	ASP226
B	GLU252
B	GLU280

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	THR136-GLY161

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"18754693","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18754693","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"MAY-2008","submissionDatabase":"PDB data bank","title":"Crystal structure of L-rhamnonate dehydratase from Salmonella typhimurium complexed with Mg and D-malate.","authors":["Fedorov A.A.","Fedorov E.V.","Sauder J.M.","Burley S.K.","Gerlt J.A.","Almo S.C."]}},{"source":"PDB","id":"3D47","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"MAY-2008","submissionDatabase":"PDB data bank","title":"Crystal structure of L-rhamnonate dehydratase from Salmonella typhimurium complexed with Mg and D-malate.","authors":["Fedorov A.A.","Fedorov E.V.","Sauder J.M.","Burley S.K.","Gerlt J.A.","Almo S.C."]}},{"source":"PDB","id":"3D47","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18754693","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2006","submissionDatabase":"PDB data bank","title":"Crystal Structure of L-rhamnonate dehydratase from Salmonella Typhimurium Lt2.","authors":["Patskovsky Y.","Malashkevich V.N.","Sauder J.M.","Dickey M.","Ozyurt S.","Wasserman S.R.","Gerlt J.","Almo S.C."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2008","submissionDatabase":"PDB data bank","title":"Crystal structure of L-rhamnonate dehydratase from Salmonella typhimurium complexed with Mg and L-tartrate.","authors":["Fedorov A.A.","Fedorov E.V.","Sauder J.M.","Burley S.K.","Gerlt J.A.","Almo S.C."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2008","submissionDatabase":"PDB data bank","title":"Crystal structure of L-rhamnonate dehydratase from Salmonella typhimurium complexed with Mg and D-malate.","authors":["Fedorov A.A.","Fedorov E.V.","Sauder J.M.","Burley S.K.","Gerlt J.A.","Almo S.C."]}},{"source":"PDB","id":"2GSH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BOX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CXO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3D46","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3D47","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18754693","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2GSH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BOX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CXO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3D46","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3D47","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18754693","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Site: {"description":"Increases basicity of active site His","evidences":[{"source":"PubMed","id":"18754693","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"18754693","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 962

Chain	Residue	Details
A	ASP226	metal ligand
A	GLU252	metal ligand
A	GLU280	metal ligand
A	ASP302	increase acidity, increase basicity, modifies pKa
A	HIS329	proton acceptor, proton donor, proton relay
A	GLU349	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	6
Details	M-CSA 962

Chain	Residue	Details
B	ASP226	metal ligand
B	GLU252	metal ligand
B	GLU280	metal ligand
B	ASP302	increase acidity, increase basicity, modifies pKa
B	HIS329	proton acceptor, proton donor, proton relay
B	GLU349	electrostatic stabiliser

---