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 | 23 |
Details | BINDING SITE FOR RESIDUE GG9 A 501 |
Chain | Residue |
A | LYS22 |
A | GLN171 |
A | SER197 |
A | TYR200 |
A | ASP313 |
A | ASN336 |
A | LYS340 |
A | ARG344 |
A | HIS385 |
A | ARG386 |
A | LYS411 |
A | SER23 |
A | HOH525 |
A | HOH534 |
A | HOH550 |
A | HOH646 |
A | ARG27 |
A | ASN94 |
A | GLY96 |
A | THR97 |
A | ARG124 |
A | SER169 |
A | SER170 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FMT A 502 |
Chain | Residue |
A | LYS373 |
A | LEU374 |
A | SER397 |
A | ASP398 |
A | HOH603 |
A | HOH730 |
A | HOH838 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT A 503 |
Chain | Residue |
A | ALA380 |
A | TYR382 |
A | HOH584 |
A | HOH735 |
A | HOH834 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT A 504 |
Chain | Residue |
A | THR5 |
A | ARG152 |
A | THR402 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT A 505 |
Chain | Residue |
A | THR58 |
A | SER63 |
A | TYR64 |
A | HOH627 |
A | HOH887 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT A 506 |
Chain | Residue |
A | ARG298 |
A | LEU301 |
A | HOH869 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT A 507 |
Chain | Residue |
A | THR65 |
A | LEU66 |
A | SER67 |
A | ARG72 |
A | HOH786 |
A | HOH913 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT A 508 |
Chain | Residue |
A | ASP13 |
A | GLY14 |
A | THR259 |
A | HOH954 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT A 509 |
Chain | Residue |
A | PRO199 |
A | HOH561 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT A 510 |
Chain | Residue |
A | LYS38 |
A | TYR335 |
A | HIS363 |
A | HOH848 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT A 511 |
Chain | Residue |
A | ARG134 |
A | LEU135 |
A | HOH695 |
A | HOH910 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FMT A 512 |
Chain | Residue |
A | PRO19 |
A | PHE413 |
A | PRO414 |
A | ASP415 |
A | HOH635 |
A | HOH645 |
A | HOH732 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT A 513 |
Chain | Residue |
A | THR263 |
A | GLY264 |
A | HOH549 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT A 514 |
Chain | Residue |
A | GLU358 |
A | GLU360 |
A | ARG367 |
A | THR369 |
A | HOH654 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT A 515 |
Chain | Residue |
A | HIS52 |
A | ASN94 |
A | GLU118 |
A | HOH558 |
A | HOH847 |
Functional Information from PROSITE/UniProt
site_id | PS00104 |
Number of Residues | 15 |
Details | EPSP_SYNTHASE_1 EPSP synthase signature 1. LFlGNAGTAMRpLaA |
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 |