2O0Z

Mycobacterium tuberculosis epsp synthase in complex with product (EPS)

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	10
Details	BINDING SITE FOR RESIDUE SO4 A 502

Chain	Residue
A	ARG68
A	HOH742
A	GLY142
A	THR143
A	GLY144
A	HOH542
A	HOH572
A	HOH652
A	HOH655
A	HOH726

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 503

Chain	Residue
A	ARG278
A	HIS286
A	ARG379
A	HOH540
A	HOH644
A	HOH903

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 A 504

Chain	Residue
A	LYS23
A	ASP54
A	LEU94
A	GLY96
A	THR97
A	ARG124
A	GLN169
A	GLU341
A	LYS410
A	HOH1022

---

site_id	AC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE EPS A 501

Chain	Residue
A	LYS23
A	SER24
A	ARG28
A	SER167
A	SER168
A	GLN169
A	SER196
A	HIS199
A	GLU311
A	HIS336
A	HIS340
A	GLU341
A	ARG344
A	HIS384
A	ARG385
A	HOH505
A	HOH509
A	HOH584
A	HOH596
A	HOH614

---

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

---