4RIZ
The crystal structure of Y333Q mutant pyridoxal-dependent decarboxylase from Sphaerobacter thermophilus dsm 20745
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016830 | molecular_function | carbon-carbon lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016830 | molecular_function | carbon-carbon lyase activity |
| C | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0019752 | biological_process | carboxylic acid metabolic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016830 | molecular_function | carbon-carbon lyase activity |
| D | 0016831 | molecular_function | carboxy-lyase activity |
| D | 0019752 | biological_process | carboxylic acid metabolic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PMP A 501 |
| Chain | Residue |
| A | GLY150 |
| A | GLN303 |
| A | LLP304 |
| A | HOH620 |
| A | HOH741 |
| A | HOH841 |
| B | THR351 |
| A | GLY151 |
| A | SER152 |
| A | HIS190 |
| A | GLY245 |
| A | THR247 |
| A | ASP272 |
| A | ALA274 |
| A | ASN301 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 502 |
| Chain | Residue |
| A | HIS353 |
| A | HOH685 |
| A | HOH686 |
| B | HIS353 |
| B | HOH629 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 501 |
| Chain | Residue |
| B | LEU136 |
| B | PHE137 |
| B | ARG286 |
| B | GLU293 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 503 |
| Chain | Residue |
| B | LEU374 |
| B | ASP377 |
| B | GLY378 |
| B | LEU381 |
| B | LEU454 |
| B | LEU455 |
| B | ASN456 |
| B | PRO457 |
| B | HOH648 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA B 504 |
| Chain | Residue |
| A | GLU171 |
| A | PRO172 |
| B | ARG180 |
| B | LEU202 |
| B | GLY203 |
| B | ALA205 |
| B | ALA206 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PMP C 2001 |
| Chain | Residue |
| C | GLY150 |
| C | GLY151 |
| C | SER152 |
| C | HIS190 |
| C | THR247 |
| C | ASP272 |
| C | ALA274 |
| C | ASN301 |
| C | GLN303 |
| C | LLP304 |
| C | HOH2217 |
| C | HOH2261 |
| D | THR351 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PMP D 501 |
| Chain | Residue |
| C | THR351 |
| C | HOH2127 |
| D | GLY150 |
| D | GLY151 |
| D | SER152 |
| D | HIS190 |
| D | GLY245 |
| D | THR247 |
| D | ASP272 |
| D | ALA274 |
| D | ASN301 |
| D | GLN303 |
| D | LLP304 |
| D | HOH694 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 502 |
| Chain | Residue |
| D | LEU136 |
| D | ARG286 |
| D | ALA290 |
| D | GLU293 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA D 503 |
| Chain | Residue |
| C | GLU171 |
| C | PRO172 |
| D | ARG180 |
| D | LEU202 |
| D | GLY203 |
| D | ALA205 |
| D | ALA206 |
