4GFS

1.8 Angstrom Crystal Structure of the 3-Dehydroquinate Dehydratase (aroD) from Salmonella typhimurium LT2 with Nickel Bound at Active Site

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	2
Details	BINDING SITE FOR RESIDUE NI A 301

Chain	Residue
A	HIS250
A	HOH457

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NI A 302

Chain	Residue
A	HIS134
A	HOH449
A	HOH460
A	HOH461
B	GLU59

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NI B 301

Chain	Residue
B	SIN305
B	HOH496
B	HOH497
B	HOH498
B	HIS143
B	LYS170

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NI B 302

Chain	Residue
A	HIS146
B	HIS146

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NI B 303

Chain	Residue
B	HIS250
B	HOH521
B	HOH522
B	HOH523
B	HOH524

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NI B 304

Chain	Residue
B	HIS134
B	HOH499
B	HOH500
B	HOH501
B	HOH502
B	HOH505

---

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SIN B 305

Chain	Residue
B	ARG48
B	ARG82
B	HIS143
B	PHE145
B	NI301
B	HOH465
B	HOH467
B	HOH496
B	HOH498

---

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	1
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

---