1P88
Substrate-induced structural changes to the isolated N-terminal domain of 5-enolpyruvylshikimate-3-phosphate synthase
Functional Information from GO Data
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 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
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 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
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 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
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 | SER169 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 457 |
Chain | Residue | Details |
A | ASP49 | metal ligand |
A | ASN94 | metal ligand |