2CY0
Crystal Structure of Shikimate 5-Dehydrogenase (AroE) from Thermus Thermophilus HB8 in complex with NADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004764 | molecular_function | shikimate 3-dehydrogenase (NADP+) activity |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019632 | biological_process | shikimate metabolic process |
| A | 0050661 | molecular_function | NADP binding |
| B | 0004764 | molecular_function | shikimate 3-dehydrogenase (NADP+) activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| B | 0009423 | biological_process | chorismate biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019632 | biological_process | shikimate metabolic process |
| B | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1401 |
| Chain | Residue |
| B | GLY125 |
| B | GLY126 |
| B | ARG151 |
| B | ARG180 |
| B | HOH1593 |
| B | HOH1594 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1402 |
| Chain | Residue |
| A | HOH1599 |
| A | HOH1612 |
| A | HOH1676 |
| A | HOH1710 |
| A | PRO192 |
| A | ARG213 |
| A | HOH1555 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAP A 1411 |
| Chain | Residue |
| A | GLY123 |
| A | ALA124 |
| A | GLY125 |
| A | GLY126 |
| A | ALA127 |
| A | ASN146 |
| A | ARG147 |
| A | THR148 |
| A | ARG151 |
| A | ALA178 |
| A | THR179 |
| A | ARG180 |
| A | VAL181 |
| A | LEU205 |
| A | VAL206 |
| A | GLY228 |
| A | LEU232 |
| A | HOH1659 |
| A | HOH1669 |
| A | HOH1671 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00222","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17825835","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00222","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17825835","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1nvt |
| Chain | Residue | Details |
| A | GLU91 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1nvt |
| Chain | Residue | Details |
| B | GLU91 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 775 |
| Chain | Residue | Details |
| A | LYS64 | proton acceptor, proton donor |
| A | ASP100 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 775 |
| Chain | Residue | Details |
| B | LYS64 | proton acceptor, proton donor |
| B | ASP100 | electrostatic stabiliser |
