2BJB

Mycobacterium Tuberculosis Epsp Synthase In Unliganded State

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0003866	molecular_function	3-phosphoshikimate 1-carboxyvinyltransferase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
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	0016740	molecular_function	transferase activity
A	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT A1424

Chain	Residue
A	TRP4
A	PRO5
A	ARG41
A	PRO228
A	ALA230
A	HOH2032
A	HOH2228

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT A1425

Chain	Residue
A	LYS410
A	HOH2054
A	HOH2218
A	HOH2229
A	ARG68
A	GLY80

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT A1426

Chain	Residue
A	ARG51
A	ARG68
A	SER79
A	PRO413
A	GLU414
A	HOH2230

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT A1427

Chain	Residue
A	ARG294
A	GLY295
A	ARG354
A	ARG379
A	HOH2162
A	HOH2231
A	HOH2232

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT A1428

Chain	Residue
A	ARG14
A	THR342
A	ASP343

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA A1429

Chain	Residue
A	ASN152
A	SER154
A	GLY356
A	PRO372

---

Functional Information from PROSITE/UniProt

site_id	PS00104
Number of Residues	15
Details	EPSP_SYNTHASE_1 EPSP synthase signature 1. VDcGLAGTVLRfVpP

Chain	Residue	Details
A	VAL90-PRO104

---

site_id	PS00885
Number of Residues	19
Details	EPSP_SYNTHASE_2 EPSP synthase signature 2. RgHETDRLaALsteInrLG

Chain	Residue	Details
A	ARG338-GLY356

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00210","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2006","submissionDatabase":"PDB data bank","title":"Complex of 3-phosphoshikimate 1-carboxyvinyltransferase.","authors":["Kachalova G.S.","Burenkov G.P.","Strizhov N.I.","Brunning M.G.","Bartunik H.D."]}},{"source":"PDB","id":"2O0E","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2006","submissionDatabase":"PDB data bank","title":"Complex of 3-phosphoshikimate 1-carboxyvinyltransferase.","authors":["Kachalova G.S.","Burenkov G.P.","Strizhov N.I.","Brunning M.G.","Bartunik H.D."]}},{"source":"PDB","id":"2O0B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O0D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O0E","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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