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 | 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 | 
| A | 0019752 | biological_process | carboxylic acid metabolic process | 
Functional Information from PDB Data
| site_id | AC1 | 
| Number of Residues | 17 | 
| Details | BINDING SITE FOR RESIDUE S3P A 701 | 
| Chain | Residue | 
| A | LYS22 | 
| A | ASP313 | 
| A | ASN336 | 
| A | LYS340 | 
| A | FMT601 | 
| A | HOH729 | 
| A | HOH730 | 
| A | HOH740 | 
| A | HOH963 | 
| A | SER23 | 
| A | ARG27 | 
| A | THR97 | 
| A | SER169 | 
| A | SER170 | 
| A | GLN171 | 
| A | SER197 | 
| A | TYR200 | 
| site_id | AC2 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE FMT A 601 | 
| Chain | Residue | 
| A | LYS22 | 
| A | ASP313 | 
| A | GLU341 | 
| A | ARG344 | 
| A | HIS385 | 
| A | ARG386 | 
| A | S3P701 | 
| site_id | AC3 | 
| Number of Residues | 9 | 
| Details | BINDING SITE FOR RESIDUE FMT A 602 | 
| Chain | Residue | 
| A | LYS22 | 
| A | ASN94 | 
| A | GLY96 | 
| A | THR97 | 
| A | ARG124 | 
| A | GLN171 | 
| A | GLU341 | 
| A | LYS411 | 
| A | HOH705 | 
| site_id | AC4 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE FMT A 603 | 
| Chain | Residue | 
| A | ALA380 | 
| A | TYR382 | 
| A | HOH779 | 
| A | HOH915 | 
| A | HOH1023 | 
| site_id | AC5 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE FMT A 604 | 
| Chain | Residue | 
| A | LYS373 | 
| A | LEU374 | 
| A | SER397 | 
| A | ASP398 | 
| A | HOH880 | 
| A | HOH1101 | 
| A | HOH1110 | 
| site_id | AC6 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE FMT A 605 | 
| Chain | Residue | 
| A | THR58 | 
| A | VAL62 | 
| A | SER63 | 
| A | TYR64 | 
| A | HOH1128 | 
| A | HOH1154 | 
| site_id | AC7 | 
| Number of Residues | 9 | 
| Details | BINDING SITE FOR RESIDUE FMT A 606 | 
| Chain | Residue | 
| A | THR5 | 
| A | THR141 | 
| A | LEU143 | 
| A | ARG152 | 
| A | PHE376 | 
| A | THR402 | 
| A | HOH1015 | 
| A | HOH1066 | 
| A | HOH1210 | 
| site_id | AC8 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE FMT A 607 | 
| Chain | Residue | 
| A | THR65 | 
| A | LEU66 | 
| A | SER67 | 
| A | ARG72 | 
| A | GLU74 | 
| A | HOH939 | 
| A | HOH1286 | 
| site_id | AC9 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE FMT A 608 | 
| Chain | Residue | 
| A | ARG11 | 
| A | ASP13 | 
| A | TYR220 | 
| A | GLN425 | 
| A | HOH1196 | 
| A | HOH1222 | 
| site_id | BC1 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE FMT A 609 | 
| Chain | Residue | 
| A | LYS38 | 
| A | TYR335 | 
| A | HIS363 | 
| A | HOH1086 | 
| A | HOH1172 | 
| A | HOH1245 | 
| A | HOH1259 | 
| site_id | BC2 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE FMT A 610 | 
| Chain | Residue | 
| A | ARG298 | 
| A | GLU300 | 
| A | LEU301 | 
| A | PHE324 | 
| A | HOH991 | 
| A | HOH1279 | 
| site_id | BC3 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE FMT A 611 | 
| Chain | Residue | 
| A | ASP13 | 
| A | GLY14 | 
| A | THR259 | 
| A | HOH1185 | 
| site_id | BC4 | 
| Number of Residues | 10 | 
| Details | BINDING SITE FOR RESIDUE FMT A 612 | 
| Chain | Residue | 
| A | HOH1198 | 
| A | HIS36 | 
| A | GLY79 | 
| A | GLY80 | 
| A | LEU182 | 
| A | SER230 | 
| A | HOH737 | 
| A | HOH888 | 
| A | HOH891 | 
| A | HOH1022 | 
Functional Information from PROSITE/UniProt
| site_id | PS00104 | 
| Number of Residues | 15 | 
| Details | EPSP_SYNTHASE_1 EPSP synthase signature 1. LFlGNAGTAMRsLaA | 
| Chain | Residue | Details | 
| A | LEU90-ALA104 |  | 
| site_id | PS00885 | 
| Number of Residues | 19 | 
| Details | EPSP_SYNTHASE_2 EPSP synthase signature 2. RvKETDRLfAMateLrkVG | 
| 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":"PubMed","id":"13129913","evidenceCode":"ECO:0000305"}]} | 
| site_id | SWS_FT_FI2 | 
| Number of Residues | 7 | 
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00210","evidenceCode":"ECO:0000255"}]} | 
| site_id | SWS_FT_FI3 | 
| Number of Residues | 8 | 
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11171958","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1G6S","evidenceCode":"ECO:0007744"}]} | 
| site_id | SWS_FT_FI4 | 
| Number of Residues | 2 | 
| Details | Site: {"description":"Modified by bromopyruvate","evidences":[{"source":"PubMed","id":"11171958","evidenceCode":"ECO:0000269"}]} | 
Catalytic Information from CSA
| site_id | CSA1 | 
| Number of Residues | 5 | 
| Details | Annotated By Reference To The Literature 1g6t | 
| Chain | Residue | Details | 
| A | LYS22 |  | 
| A | ASP313 |  | 
| A | LYS411 |  | 
| A | HIS385 |  | 
| A | GLU341 |  | 
| site_id | MCSA1 | 
| Number of Residues | 7 | 
| Details | M-CSA 457 | 
| Chain | Residue | Details | 
| A | ASP49 | metal ligand | 
| A | ASN94 | metal ligand | 
| A | ASP313 | electrostatic stabiliser, proton shuttle (general acid/base) | 
| A | GLU341 | electrostatic stabiliser, metal ligand, proton shuttle (general acid/base) | 
| A | HIS385 | steric role | 
| A | ARG386 | transition state stabiliser | 
| A | LYS411 | steric role |