2QFQ
E. coli EPSP synthase Pro101Leu liganded with S3P
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| A | 0003866 | molecular_function | 3-phosphoshikimate 1-carboxyvinyltransferase activity |
| A | 0004764 | molecular_function | shikimate 3-dehydrogenase (NADP+) activity |
| A | 0004765 | molecular_function | shikimate kinase 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE S3P A 701 |
| Chain | Residue |
| A | LYS22 |
| A | ASP313 |
| A | ASN336 |
| A | LYS340 |
| A | FMT601 |
| A | HOH707 |
| A | HOH768 |
| A | HOH959 |
| 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 | 8 |
| Details | BINDING SITE FOR RESIDUE FMT A 602 |
| Chain | Residue |
| A | LYS22 |
| A | ASN94 |
| A | GLY96 |
| A | THR97 |
| A | ARG124 |
| A | GLU341 |
| A | LYS411 |
| A | HOH746 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 603 |
| Chain | Residue |
| A | ALA380 |
| A | TYR382 |
| A | HOH827 |
| A | HOH919 |
| A | HOH1014 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A 604 |
| Chain | Residue |
| A | LYS373 |
| A | LEU374 |
| A | SER397 |
| A | ASP398 |
| A | HOH918 |
| A | HOH1060 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 605 |
| Chain | Residue |
| A | THR65 |
| A | LEU66 |
| A | SER67 |
| A | ARG72 |
| A | HOH910 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A 607 |
| Chain | Residue |
| A | THR58 |
| A | VAL62 |
| A | SER63 |
| A | TYR64 |
| A | HOH1147 |
| A | HOH1160 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A 608 |
| Chain | Residue |
| A | LYS38 |
| A | TYR335 |
| A | HIS363 |
| A | HOH1139 |
| A | HOH1156 |
| A | HOH1189 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 609 |
| Chain | Residue |
| A | ASP13 |
| A | GLY14 |
| A | THR259 |
| A | HOH1187 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT A 610 |
| Chain | Residue |
| A | THR5 |
| A | LEU143 |
| A | ARG152 |
| A | PHE376 |
| A | THR402 |
| A | HOH1238 |
| A | HOH1255 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:15736934, ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556 |
| Chain | Residue | Details |
| A | ASP313 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:15736934, ECO:0000305|PubMed:11171958 |
| Chain | Residue | Details |
| A | GLU341 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:15736934, ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556 |
| Chain | Residue | Details |
| A | LYS22 | |
| A | SER169 | |
| A | LYS340 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:15736934, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556 |
| Chain | Residue | Details |
| A | ARG27 | |
| A | SER197 | |
| A | ASN336 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:19211556 |
| Chain | Residue | Details |
| A | ARG124 | |
| A | ARG344 | |
| A | ARG386 | |
| A | LYS411 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Modified by bromopyruvate => ECO:0000269|PubMed:11171958 |
| Chain | Residue | Details |
| A | CYS408 | |
| A | LYS411 |
Catalytic Information from CSA
| 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 |
