5YHT
Crystal structure of a phosphatase from Mycobacterium tuberculosis in complex with its substrate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000105 | biological_process | L-histidine biosynthetic process |
| A | 0004401 | molecular_function | histidinol-phosphatase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008934 | molecular_function | inositol monophosphate 1-phosphatase activity |
| A | 0010125 | biological_process | mycothiol biosynthetic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016791 | molecular_function | phosphatase activity |
| A | 0042578 | molecular_function | phosphoric ester hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000105 | biological_process | L-histidine biosynthetic process |
| B | 0004401 | molecular_function | histidinol-phosphatase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008934 | molecular_function | inositol monophosphate 1-phosphatase activity |
| B | 0010125 | biological_process | mycothiol biosynthetic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016791 | molecular_function | phosphatase activity |
| B | 0042578 | molecular_function | phosphoric ester hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | GLU67 |
| A | ASP83 |
| A | ASP213 |
| A | HSA303 |
| A | HOH402 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | ILE85 |
| A | HSA303 |
| A | ASP44 |
| A | GLU67 |
| A | GLU68 |
| A | ASP83 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue HSA A 303 |
| Chain | Residue |
| A | ASP44 |
| A | GLU67 |
| A | ASP83 |
| A | ILE85 |
| A | ASP86 |
| A | GLY87 |
| A | THR88 |
| A | ASP189 |
| A | GLU206 |
| A | ASP213 |
| A | ZN301 |
| A | ZN302 |
| A | HOH401 |
| A | HOH402 |
| B | HOH404 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 A 304 |
| Chain | Residue |
| A | ARG183 |
| A | ARG185 |
| B | SER160 |
| B | SER161 |
| B | HOH403 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue HSO B 301 |
| Chain | Residue |
| A | LEU191 |
| B | PRO96 |
| B | VAL97 |
| B | LEU120 |
| B | LEU191 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 302 |
| Chain | Residue |
| B | GLU67 |
| B | ASP83 |
| B | ASP213 |
| B | PO4304 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 303 |
| Chain | Residue |
| B | ASP86 |
| B | ASP189 |
| B | ASP213 |
| B | PO4304 |
| B | HOH412 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 B 304 |
| Chain | Residue |
| B | ILE85 |
| B | ASP86 |
| B | GLY87 |
| B | THR88 |
| B | ZN302 |
| B | ZN303 |
| B | HOH403 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 B 305 |
| Chain | Residue |
| A | SER161 |
| B | ARG183 |
| B | ARG185 |
| B | HOH404 |
Functional Information from PROSITE/UniProt
| site_id | PS00629 |
| Number of Residues | 14 |
| Details | IMP_1 Inositol monophosphatase family signature 1. WiVDPIDGTknFvR |
| Chain | Residue | Details |
| A | TRP80-ARG93 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU67 | |
| B | ASP86 | |
| B | ARG185 | |
| B | ASP213 | |
| A | ASP83 | |
| A | ILE85 | |
| A | ASP86 | |
| A | ARG185 | |
| A | ASP213 | |
| B | GLU67 | |
| B | ASP83 | |
| B | ILE85 |
