2D5C
Crystal Structure of Shikimate 5-Dehydrogenase (AroE) from Thermus Thermophilus HB8 in complex with shikimate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004764 | molecular_function | shikimate 3-dehydrogenase (NADP+) activity |
| 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 | 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 | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1401 |
| Chain | Residue |
| A | LYS109 |
| B | ARG162 |
| B | HOH1480 |
| A | PRO192 |
| A | ALA193 |
| A | ARG213 |
| A | HOH1413 |
| A | HOH1429 |
| A | HOH1466 |
| A | HOH1550 |
| A | HOH1642 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1402 |
| Chain | Residue |
| A | ARG241 |
| A | LEU242 |
| B | GLN89 |
| B | VAL90 |
| B | GLU91 |
| B | HOH1409 |
| B | HOH1413 |
| B | HOH1454 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1403 |
| Chain | Residue |
| A | GLN226 |
| A | THR227 |
| A | ARG258 |
| A | HOH1572 |
| A | HOH1590 |
| A | HOH1635 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1404 |
| Chain | Residue |
| A | GLU157 |
| B | ARG180 |
| B | ALA188 |
| B | SER189 |
| B | THR212 |
| B | ARG213 |
| B | PHE214 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SKM A 301 |
| Chain | Residue |
| A | VAL6 |
| A | SER14 |
| A | SER16 |
| A | ASN58 |
| A | LEU59 |
| A | THR60 |
| A | LYS64 |
| A | ASN85 |
| A | ASP100 |
| A | TYR207 |
| A | GLN235 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SKM B 302 |
| Chain | Residue |
| B | SER14 |
| B | SER16 |
| B | ASN58 |
| B | THR60 |
| B | LYS64 |
| B | ASN85 |
| B | ASP100 |
| B | GLN235 |
| B | HOH1421 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|PubMed:17825835 |
| Chain | Residue | Details |
| A | LYS64 | |
| B | LYS64 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|PubMed:17825835 |
| Chain | Residue | Details |
| A | SER14 | |
| A | GLN235 | |
| B | SER14 | |
| B | THR60 | |
| B | ASN85 | |
| B | ASP100 | |
| B | GLY123 | |
| B | ASN146 | |
| B | LEU205 | |
| B | TYR207 | |
| B | GLY228 | |
| A | THR60 | |
| B | GLN235 | |
| A | ASN85 | |
| A | ASP100 | |
| A | GLY123 | |
| A | ASN146 | |
| A | LEU205 | |
| A | TYR207 | |
| A | GLY228 |
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 |
