1SHK
THE THREE-DIMENSIONAL STRUCTURE OF SHIKIMATE KINASE FROM ERWINIA CHRYSANTHEMI
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0016310 | biological_process | phosphorylation |
A | 0019752 | biological_process | carboxylic acid metabolic process |
A | 0046872 | molecular_function | metal ion 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 | 0016310 | biological_process | phosphorylation |
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 | 8 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY12 | |
A | THR16 | |
A | ASP32 | |
A | GLN155 | |
B | GLY12 | |
B | THR16 | |
B | ASP32 | |
B | GLN155 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | ASP34 | |
A | ARG58 | |
A | ARG139 | |
B | ASP34 | |
B | ARG58 | |
B | ARG139 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLY79 | |
A | ARG120 | |
B | GLY79 | |
B | ARG120 |