1SHK
THE THREE-DIMENSIONAL STRUCTURE OF SHIKIMATE KINASE FROM ERWINIA CHRYSANTHEMI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004765 | molecular_function | shikimate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004765 | molecular_function | shikimate kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| 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 | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 902 |
| Chain | Residue |
| A | GLN144 |
| A | ALA147 |
| A | HOH995 |
| A | HOH1026 |
| A | HOH1027 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 903 |
| Chain | Residue |
| A | ARG92 |
| A | ALA93 |
| A | GLY95 |
| B | ARG92 |
| B | GLY95 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 901 |
| Chain | Residue |
| B | GLN144 |
| B | ALA147 |
| B | HOH954 |
| B | HOH955 |
| B | HOH958 |
| site_id | PIP |
| Number of Residues | 4 |
| Details | A WALKER TYPE A MOTIF FORMS THE P-LOOP WHICH IS THE BINDING SITE FOR THE PHOSPHATES OF ATP. |
| Chain | Residue |
| B | GLY14 |
| B | LYS15 |
| B | THR16 |
| B | GLY9 |
| site_id | POP |
| Number of Residues | 4 |
| Details | A WALKER TYPE A MOTIF FORMS THE P-LOOP WHICH IS THE BINDING SITE FOR THE PHOSPHATES OF ATP. |
| Chain | Residue |
| A | GLY9 |
| A | GLY14 |
| A | LYS15 |
| A | THR16 |
| site_id | SAS |
| Number of Residues | 4 |
| Details | THE ELECTRON DENSITY FOR SHIKIMATE WAS AMBIGUOUS PREVENTING ITS INCLUSION IN THE MODEL. THE LISTED RESIDUES ARE GROUPED AROUND THE DENSITY AND ARE MOST LIKELY TO BE PART OF THE SHIKIMATE BINDING. |
| Chain | Residue |
| A | ASP34 |
| A | GLU61 |
| A | ARG58 |
| A | ARG139 |
| site_id | SBS |
| Number of Residues | 4 |
| Details | THE ELECTRON DENSITY FOR SHIKIMATE WAS AMBIGUOUS PREVENTING ITS INCLUSION IN THE MODEL. THE LISTED RESIDUES ARE GROUPED AROUND THE DENSITY AND ARE MOST LIKELY TO BE PART OF THE SHIKIMATE BINDING. |
| Chain | Residue |
| B | ASP34 |
| B | GLU61 |
| B | ARG58 |
| B | ARG139 |
Functional Information from PROSITE/UniProt
| site_id | PS01128 |
| Number of Residues | 25 |
| Details | SHIKIMATE_KINASE Shikimate kinase signature. RrrEseaLqavatpnr....VVAtGGGmV |
| Chain | Residue | Details |
| A | ARG58-VAL82 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
