1RKV
Structure of Phosphate complex of ThrH from 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 | 0009088 | biological_process | 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 | 0009088 | biological_process | 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 | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 320 |
| Chain | Residue |
| A | ASP7 |
| A | LEU8 |
| A | GLU9 |
| A | SER90 |
| A | ASP91 |
| A | LYS133 |
| A | MG401 |
| A | HOH546 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | GLU9 |
| A | ASP152 |
| A | PO4320 |
| A | HOH526 |
| A | HOH538 |
| A | ASP7 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 402 |
| Chain | Residue |
| A | ASP152 |
| A | HOH572 |
| A | HOH649 |
| A | HOH717 |
| A | HOH789 |
| A | HOH794 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 321 |
| Chain | Residue |
| B | ASP7 |
| B | LEU8 |
| B | GLU9 |
| B | SER90 |
| B | ASP91 |
| B | LYS133 |
| B | MG403 |
| B | HOH701 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 403 |
| Chain | Residue |
| B | ASP7 |
| B | GLU9 |
| B | ASP152 |
| B | PO4321 |
| B | HOH542 |
| B | HOH552 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 404 |
| Chain | Residue |
| A | ASN174 |
| B | ASP152 |
| B | HIS170 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 901 |
| Chain | Residue |
| A | GLN129 |
| A | LYS130 |
| A | TYR144 |
| A | HOH642 |
| B | GLN129 |
| B | LYS130 |
| B | TYR144 |
| B | HOH735 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 904 |
| Chain | Residue |
| A | THR24 |
| A | GLY25 |
| A | ILE26 |
| A | ASP78 |
| A | ARG81 |
| A | HOH515 |
| A | HOH536 |
| B | GLY105 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 902 |
| Chain | Residue |
| B | GLU9 |
| B | TRP17 |
| B | TYR39 |
| B | THR92 |
| B | PHE93 |
| B | HOH825 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 903 |
| Chain | Residue |
| B | ASP0 |
| B | MET1 |
| B | GLU2 |
| B | ARG201 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:14699121 |
| Chain | Residue | Details |
| A | ASP7 | |
| B | ASP7 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:14699121 |
| Chain | Residue | Details |
| A | GLU9 | |
| B | GLU9 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14699121 |
| Chain | Residue | Details |
| A | ASP7 | |
| B | GLU9 | |
| B | ASP152 | |
| A | GLU9 | |
| A | ASP152 | |
| B | ASP7 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q58989 |
| Chain | Residue | Details |
| A | SER90 | |
| A | LYS133 | |
| A | ASN155 | |
| B | GLU15 | |
| B | ARG46 | |
| B | SER90 | |
| B | LYS133 | |
| B | ASN155 | |
| A | GLU15 | |
| A | ARG46 |
