3FK0
E. coli EPSP synthase (TIPS mutation) 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 | 17 |
Details | BINDING SITE FOR RESIDUE S3P A 428 |
Chain | Residue |
A | LYS22 |
A | ASP313 |
A | ASN336 |
A | LYS340 |
A | FMT430 |
A | HOH551 |
A | HOH553 |
A | HOH825 |
A | HOH839 |
A | SER23 |
A | ARG27 |
A | ILE97 |
A | SER169 |
A | SER170 |
A | GLN171 |
A | SER197 |
A | TYR200 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT A 429 |
Chain | Residue |
A | ALA380 |
A | TYR382 |
A | HOH467 |
A | HOH558 |
A | HOH807 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FMT A 430 |
Chain | Residue |
A | LYS22 |
A | ASP313 |
A | GLU341 |
A | ARG344 |
A | HIS385 |
A | ARG386 |
A | S3P428 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT A 431 |
Chain | Residue |
A | LYS373 |
A | LEU374 |
A | SER397 |
A | ASP398 |
A | HOH685 |
A | HOH843 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT A 432 |
Chain | Residue |
A | THR65 |
A | LEU66 |
A | SER67 |
A | ARG72 |
A | FMT436 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT A 433 |
Chain | Residue |
A | ARG298 |
A | GLU300 |
A | LEU301 |
A | PHE324 |
A | HOH918 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT A 434 |
Chain | Residue |
A | THR58 |
A | VAL62 |
A | SER63 |
A | TYR64 |
A | HOH850 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT A 435 |
Chain | Residue |
A | THR5 |
A | LEU143 |
A | ARG152 |
A | PHE376 |
A | THR402 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT A 436 |
Chain | Residue |
A | FMT432 |
A | HOH513 |
A | HOH701 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT A 437 |
Chain | Residue |
A | LYS38 |
A | HIS363 |
A | HOH937 |
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 |