4GUI

1.78 Angstrom Crystal Structure of the Salmonella enterica 3-Dehydroquinate Dehydratase (aroD) in Complex with Quinate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003855	molecular_function	3-dehydroquinate dehydratase activity
A	0005829	cellular_component	cytosol
A	0008652	biological_process	amino acid biosynthetic process
A	0009073	biological_process	aromatic amino acid family biosynthetic process
A	0009423	biological_process	chorismate biosynthetic process
A	0016829	molecular_function	lyase activity
A	0046279	biological_process	3,4-dihydroxybenzoate biosynthetic process
B	0003855	molecular_function	3-dehydroquinate dehydratase activity
B	0005829	cellular_component	cytosol
B	0008652	biological_process	amino acid biosynthetic process
B	0009073	biological_process	aromatic amino acid family biosynthetic process
B	0009423	biological_process	chorismate biosynthetic process
B	0016829	molecular_function	lyase activity
B	0046279	biological_process	3,4-dihydroxybenzoate biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE QIC A 301

Chain	Residue
A	SER21
A	SER232
A	ALA233
A	GLN236
A	HOH447
A	GLU46
A	ARG48
A	ARG82
A	HIS143
A	LYS170
A	MET205
A	ARG213
A	PHE225

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NI A 302

Chain	Residue
A	HIS250
A	HOH483
A	HOH484
A	HOH485
A	HOH486
A	HOH487

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NI A 303

Chain	Residue
A	ASP106
A	HIS134
A	HOH489
A	HOH490
A	HOH491
B	GLU59

---

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE QIC B 301

Chain	Residue
B	LYS170
B	MET203
B	MET205
B	ARG213
B	PHE225
B	GLN236
B	HOH423
B	HOH480
B	HOH503
B	HOH543
B	HOH545

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NI B 302

Chain	Residue
B	HIS250
B	HOH504
B	HOH505
B	HOH506
B	HOH507
B	HOH508

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NI B 303

Chain	Residue
B	HIS134
B	HOH509
B	HOH510
B	HOH511
B	HOH512
B	HOH533

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NI B 304

Chain	Residue
B	HIS132
B	HOH513
B	HOH514
B	HOH519

---

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NI B 305

Chain	Residue
A	HIS146
B	HIS146
B	HOH515
B	HOH516
B	HOH517

---

Functional Information from PROSITE/UniProt

site_id	PS01028
Number of Residues	31
Details	DEHYDROQUINASE_I Dehydroquinase class I active site. DLELftgddevkatvgyahqhnvaVImSNHD

Chain	Residue	Details
A	ASP114-ASP144

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21087925","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23341204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24437575","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of the 3-dehydroquinate dehydratase (aroD) from Salmonella typhimurium LT2 with citrate bound to the active Site.","authors":["Minasov G.","Light S.H.","Shuvalova L.","Papazisi L.","Anderson W.F."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2012","submissionDatabase":"PDB data bank","title":"1.8 angstrom crystal structure of the 3-dehydroquinate dehydratase (aroD) from Salmonella typhimurium LT2 with nickel bound at active site.","authors":["Light S.H.","Minasov G.","Krishna S.N.","Shuvalova L.","Kwon K.","Lavie A.","Anderson W.F."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21087925","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23341204","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of the 3-dehydroquinate dehydratase (aroD) from Salmonella typhimurium LT2 with citrate bound to the active Site.","authors":["Minasov G.","Light S.H.","Shuvalova L.","Papazisi L.","Anderson W.F."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of the 3-dehydroquinate dehydratase (aroD) from Salmonella enterica typhimurium LT2 with malonate and boric acid at the active site.","authors":["Light S.H.","Minasov G.","Duban M.-E.","Halavaty A.S.","Krishna S.N.","Shuvalova L.","Kwon K.","Anderson W.F."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2012","submissionDatabase":"PDB data bank","title":"1.8 angstrom crystal structure of the 3-dehydroquinate dehydratase (aroD) from Salmonella typhimurium LT2 with nickel bound at active site.","authors":["Light S.H.","Minasov G.","Krishna S.N.","Shuvalova L.","Kwon K.","Lavie A.","Anderson W.F."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21087925","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24437575","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of the 3-dehydroquinate dehydratase (aroD) from Salmonella typhimurium LT2 with citrate bound to the active Site.","authors":["Minasov G.","Light S.H.","Shuvalova L.","Papazisi L.","Anderson W.F."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of the 3-dehydroquinate dehydratase (aroD) from Salmonella enterica typhimurium LT2 with malonate and boric acid at the active site.","authors":["Light S.H.","Minasov G.","Duban M.-E.","Halavaty A.S.","Krishna S.N.","Shuvalova L.","Kwon K.","Anderson W.F."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21087925","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23341204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24437575","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of the 3-dehydroquinate dehydratase (aroD) from Salmonella typhimurium LT2 with citrate bound to the active Site.","authors":["Minasov G.","Light S.H.","Shuvalova L.","Papazisi L.","Anderson W.F."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of the 3-dehydroquinate dehydratase (aroD) from Salmonella enterica typhimurium LT2 with malonate and boric acid at the active site.","authors":["Light S.H.","Minasov G.","Duban M.-E.","Halavaty A.S.","Krishna S.N.","Shuvalova L.","Kwon K.","Anderson W.F."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21087925","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23341204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24437575","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of the 3-dehydroquinate dehydratase (aroD) from Salmonella typhimurium LT2 with citrate bound to the active Site.","authors":["Minasov G.","Light S.H.","Shuvalova L.","Papazisi L.","Anderson W.F."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of the 3-dehydroquinate dehydratase (aroD) from Salmonella enterica typhimurium LT2 with malonate and boric acid at the active site.","authors":["Light S.H.","Minasov G.","Duban M.-E.","Halavaty A.S.","Krishna S.N.","Shuvalova L.","Kwon K.","Anderson W.F."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2012","submissionDatabase":"PDB data bank","title":"1.8 angstrom crystal structure of the 3-dehydroquinate dehydratase (aroD) from Salmonella typhimurium LT2 with nickel bound at active site.","authors":["Light S.H.","Minasov G.","Krishna S.N.","Shuvalova L.","Kwon K.","Lavie A.","Anderson W.F."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21087925","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24437575","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of the 3-dehydroquinate dehydratase (aroD) from Salmonella typhimurium LT2 with citrate bound to the active Site.","authors":["Minasov G.","Light S.H.","Shuvalova L.","Papazisi L.","Anderson W.F."]}}]}

Chain

Residue

Details

---