1RMT
Crystal structure of AphA class B acid phosphatase/phosphotransferase complexed with adenosine.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003993 | molecular_function | acid phosphatase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0036424 | molecular_function | L-phosphoserine phosphatase activity |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003993 | molecular_function | acid phosphatase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0036424 | molecular_function | L-phosphoserine phosphatase activity |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003993 | molecular_function | acid phosphatase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| C | 0036424 | molecular_function | L-phosphoserine phosphatase activity |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003993 | molecular_function | acid phosphatase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| D | 0036424 | molecular_function | L-phosphoserine phosphatase activity |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0042802 | molecular_function | identical protein binding |
| D | 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 1413 |
| Chain | Residue |
| A | ASP44 |
| A | ASP46 |
| A | ASP167 |
| A | HOH1775 |
| A | HOH1797 |
| A | HOH1812 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1414 |
| Chain | Residue |
| B | HOH1800 |
| B | HOH1818 |
| B | HOH1831 |
| B | ASP44 |
| B | ASP46 |
| B | ASP167 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 1415 |
| Chain | Residue |
| C | ASP44 |
| C | ASP46 |
| C | ASP167 |
| C | HOH1750 |
| C | HOH1771 |
| C | HOH1787 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 1416 |
| Chain | Residue |
| D | ASP44 |
| D | ASP46 |
| D | ASP167 |
| D | HOH1778 |
| D | HOH1797 |
| D | HOH1811 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADN A 1501 |
| Chain | Residue |
| A | ASP46 |
| A | PHE56 |
| A | TYR70 |
| A | LEU71 |
| A | TRP77 |
| A | GLY113 |
| A | ARG114 |
| A | THR192 |
| A | TYR193 |
| A | HOH1505 |
| A | HOH1548 |
| A | HOH1813 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADN B 1502 |
| Chain | Residue |
| B | PHE56 |
| B | GLU68 |
| B | TYR70 |
| B | LEU71 |
| B | THR192 |
| B | TYR193 |
| B | LYS194 |
| B | HOH1540 |
| B | HOH1706 |
| B | HOH1813 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADN C 1503 |
| Chain | Residue |
| C | ASP46 |
| C | PHE56 |
| C | TYR70 |
| C | LEU71 |
| C | TRP77 |
| C | GLY113 |
| C | ARG114 |
| C | ASP145 |
| C | THR192 |
| C | TYR193 |
| C | HOH1531 |
| C | HOH1608 |
| C | HOH1750 |
| C | HOH1787 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADN D 1504 |
| Chain | Residue |
| D | ASP46 |
| D | PHE56 |
| D | LEU71 |
| D | TRP77 |
| D | GLY113 |
| D | ASP145 |
| D | THR192 |
| D | TYR193 |
| D | HOH1604 |
| D | HOH1647 |
| D | HOH1675 |
| D | HOH1714 |
| D | HOH1797 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| A | ASP44 | |
| B | ASP44 | |
| C | ASP44 | |
| D | ASP44 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | ASP46 | |
| B | ASP46 | |
| C | ASP46 | |
| D | ASP46 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP44 | |
| B | ASP167 | |
| C | ASP44 | |
| C | ASP46 | |
| C | THR112 | |
| C | LYS152 | |
| C | ASP167 | |
| D | ASP44 | |
| D | ASP46 | |
| D | THR112 | |
| D | LYS152 | |
| A | ASP46 | |
| D | ASP167 | |
| A | THR112 | |
| A | LYS152 | |
| A | ASP167 | |
| B | ASP44 | |
| B | ASP46 | |
| B | THR112 | |
| B | LYS152 |
