1NVT
Crystal structure of Shikimate Dehydrogenase (AROE or MJ1084) in complex with NADP+
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 | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 290 |
| Chain | Residue |
| A | HIS19 |
| B | ASN279 |
| B | ASP283 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 291 |
| Chain | Residue |
| B | GLU22 |
| B | HIS23 |
| B | ASP190 |
| B | ASP192 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAP A 288 |
| Chain | Residue |
| A | GLY137 |
| A | ALA139 |
| A | ASN157 |
| A | ARG158 |
| A | THR159 |
| A | LYS162 |
| A | ALA200 |
| A | THR201 |
| A | PRO202 |
| A | ILE203 |
| A | MET205 |
| A | LEU229 |
| A | ILE230 |
| A | TYR231 |
| A | GLY252 |
| A | MET255 |
| A | LEU256 |
| A | HOH296 |
| A | HOH316 |
| A | HOH333 |
| B | ASN246 |
| B | LYS248 |
| A | GLY135 |
| A | ALA136 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAP B 289 |
| Chain | Residue |
| B | ILE72 |
| B | GLY135 |
| B | ALA136 |
| B | GLY137 |
| B | GLY138 |
| B | ALA139 |
| B | ASN157 |
| B | ARG158 |
| B | THR159 |
| B | LYS162 |
| B | ALA200 |
| B | THR201 |
| B | PRO202 |
| B | ILE203 |
| B | MET205 |
| B | LEU229 |
| B | TYR231 |
| B | GLY252 |
| B | MET255 |
| B | LEU256 |
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 |
| Chain | Residue | Details |
| A | LYS75 | |
| B | LYS75 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222 |
| Chain | Residue | Details |
| A | SER24 | |
| B | ASP111 | |
| B | TYR231 | |
| B | GLY252 | |
| A | THR71 | |
| A | ASN96 | |
| A | ASP111 | |
| A | TYR231 | |
| A | GLY252 | |
| B | SER24 | |
| B | THR71 | |
| B | ASN96 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|PubMed:12906831 |
| Chain | Residue | Details |
| A | GLY135 | |
| A | ASN157 | |
| A | THR201 | |
| B | GLY135 | |
| B | ASN157 | |
| B | THR201 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12906831 |
| Chain | Residue | Details |
| A | MET205 | |
| A | LEU229 | |
| B | MET205 | |
| B | LEU229 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 12624088, 12906831, 12637497, 12837789 |
| Chain | Residue | Details |
| A | ASP102 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 12624088, 12906831, 12637497, 12837789 |
| Chain | Residue | Details |
| B | ASP102 |
