1RKU
Crystal Structure of ThrH gene product of Pseudomonas Aeruginosa
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004413 | molecular_function | homoserine kinase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006564 | biological_process | L-serine biosynthetic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009088 | biological_process | L-threonine biosynthetic process |
| A | 0016311 | biological_process | dephosphorylation |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0036424 | molecular_function | L-phosphoserine phosphatase activity |
| A | 0043899 | molecular_function | phosphoserine:homoserine phosphotransferase activity |
| A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| A | 0046820 | molecular_function | 4-amino-4-deoxychorismate synthase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004413 | molecular_function | homoserine kinase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006564 | biological_process | L-serine biosynthetic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009088 | biological_process | L-threonine biosynthetic process |
| B | 0016311 | biological_process | dephosphorylation |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0036424 | molecular_function | L-phosphoserine phosphatase activity |
| B | 0043899 | molecular_function | phosphoserine:homoserine phosphotransferase activity |
| B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| B | 0046820 | molecular_function | 4-amino-4-deoxychorismate synthase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 301 |
| Chain | Residue |
| A | ASP7 |
| A | GLU9 |
| A | ASP152 |
| A | HOH719 |
| A | HOH814 |
| A | HOH843 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 302 |
| Chain | Residue |
| A | HOH845 |
| A | ASP152 |
| A | HOH725 |
| A | HOH844 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 303 |
| Chain | Residue |
| B | ASP7 |
| B | GLU9 |
| B | ASP152 |
| B | HOH748 |
| B | HOH780 |
| B | HOH846 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 304 |
| Chain | Residue |
| B | ASP152 |
| B | HOH749 |
| B | HOH813 |
| B | HOH840 |
| B | HOH847 |
| B | HOH872 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 401 |
| Chain | Residue |
| A | THR24 |
| A | GLY25 |
| A | ILE26 |
| A | ASP78 |
| A | ARG81 |
| A | HOH552 |
| A | HOH866 |
| B | GLY105 |
| B | PHE106 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 404 |
| Chain | Residue |
| A | ASP0 |
| A | MET1 |
| A | GLU2 |
| A | GLN85 |
| A | ARG201 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 405 |
| Chain | Residue |
| A | GLN129 |
| A | LYS130 |
| A | HOH643 |
| B | LYS130 |
| B | TYR144 |
| B | HOH581 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 407 |
| Chain | Residue |
| A | ASP91 |
| A | ASP131 |
| A | PRO132 |
| A | LYS133 |
| A | ARG134 |
| A | THR158 |
| A | HOH512 |
| A | HOH727 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO B 402 |
| Chain | Residue |
| A | GLY25 |
| A | ASP27 |
| A | LYS30 |
| A | HOH531 |
| B | VAL74 |
| B | ASP78 |
| B | ARG81 |
| B | GLN103 |
| B | LEU104 |
| B | GLY105 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 403 |
| Chain | Residue |
| B | ASP0 |
| B | MET1 |
| B | GLU2 |
| B | ARG83 |
| B | GLN85 |
| B | ARG201 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 406 |
| Chain | Residue |
| B | GLU75 |
| B | ASP78 |
| B | GLU82 |
| B | HOH576 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"14699121","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"14699121","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14699121","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q58989","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
