2HK7
Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with mercury at 2.5 angstrom resolution
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 | 3 |
Details | BINDING SITE FOR RESIDUE HG A 270 |
Chain | Residue |
A | HIS18 |
A | HOH321 |
A | HOH322 |
site_id | AC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE HG A 271 |
Chain | Residue |
A | MET1 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE HG A 272 |
Chain | Residue |
A | CYS253 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE HG B 270 |
Chain | Residue |
B | HIS18 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE HG B 271 |
Chain | Residue |
B | MET1 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE HG B 272 |
Chain | Residue |
B | CYS253 |
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:0000305|PubMed:17649975 |
Chain | Residue | Details |
A | LYS70 | |
B | LYS70 |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|PubMed:17649975 |
Chain | Residue | Details |
A | SER19 | |
B | SER19 | |
B | ASP82 | |
B | ASN91 | |
B | ASP106 | |
B | GLY130 | |
B | ILE214 | |
B | TYR216 | |
B | GLY235 | |
B | GLN242 | |
A | ASP82 | |
A | ASN91 | |
A | ASP106 | |
A | GLY130 | |
A | ILE214 | |
A | TYR216 | |
A | GLY235 | |
A | GLN242 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222 |
Chain | Residue | Details |
A | THR66 | |
B | THR66 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000305|PubMed:17649975 |
Chain | Residue | Details |
A | ASN153 | |
B | ASN153 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1nvt |
Chain | Residue | Details |
A | ASN97 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1nvt |
Chain | Residue | Details |
B | ASN97 |