4B5X
Crystal structures of divalent metal dependent pyruvate aldolase (HpaI), mutant D42A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0010124 | biological_process | phenylacetate catabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016832 | molecular_function | aldehyde-lyase activity |
| A | 0018802 | molecular_function | 2,4-dihydroxyhept-2-ene-1,7-dioate aldolase activity |
| A | 0019439 | biological_process | obsolete aromatic compound catabolic process |
| A | 0043863 | molecular_function | 4-hydroxy-2-ketopimelate aldolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0010124 | biological_process | phenylacetate catabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016832 | molecular_function | aldehyde-lyase activity |
| B | 0018802 | molecular_function | 2,4-dihydroxyhept-2-ene-1,7-dioate aldolase activity |
| B | 0019439 | biological_process | obsolete aromatic compound catabolic process |
| B | 0043863 | molecular_function | 4-hydroxy-2-ketopimelate aldolase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1254 |
| Chain | Residue |
| A | TYR26 |
| B | HOH2106 |
| B | GLU44 |
| B | HIS45 |
| B | ASP84 |
| B | VAL85 |
| B | ALA123 |
| B | ARG124 |
| B | HOH2065 |
| B | HOH2104 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1255 |
| Chain | Residue |
| A | SER24 |
| A | TYR26 |
| A | HOH2071 |
| B | LEU22 |
| B | SER23 |
| B | SER24 |
| B | HIS45 |
| B | HOH2385 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1252 |
| Chain | Residue |
| A | HIS45 |
| A | ASP84 |
| A | VAL85 |
| A | ALA123 |
| A | ARG124 |
| A | HOH2064 |
| A | HOH2212 |
| A | HOH2291 |
| B | TYR26 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1253 |
| Chain | Residue |
| A | LEU22 |
| A | SER23 |
| A | SER24 |
| A | HIS45 |
| A | HOH2117 |
| A | HOH2446 |
| B | SER24 |
| B | TYR26 |
| B | HOH2385 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1254 |
| Chain | Residue |
| A | LYS6 |
| A | ARG109 |
| A | GLU164 |
| A | ASP167 |
| A | HOH2319 |
| A | HOH2345 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1256 |
| Chain | Residue |
| B | LYS6 |
| B | ARG109 |
| B | GLU164 |
| B | ASP167 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1257 |
| Chain | Residue |
| B | ARG70 |
| B | LYS80 |
| B | GLY117 |
| B | GLY119 |
| B | GLU149 |
| B | ASP175 |
| B | HOH2148 |
| B | HOH2236 |
| B | HOH2386 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1255 |
| Chain | Residue |
| A | ARG70 |
| A | LYS80 |
| A | GLY117 |
| A | GLY119 |
| A | GLU149 |
| A | ASP175 |
| A | HOH2447 |
| A | HOH2448 |
| A | HOH2449 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 1258 |
| Chain | Residue |
| A | ARG127 |
| A | HOH2294 |
| B | PRO62 |
| B | TYR63 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1256 |
| Chain | Residue |
| A | PRO62 |
| A | TYR63 |
| A | HOH2081 |
| B | ARG127 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01292 |
| Chain | Residue | Details |
| A | HIS45 | |
| B | HIS45 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01292 |
| Chain | Residue | Details |
| A | GLN147 | |
| A | GLU149 | |
| A | ALA174 | |
| A | ASP175 | |
| B | GLN147 | |
| B | GLU149 | |
| B | ALA174 | |
| B | ASP175 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01292 |
| Chain | Residue | Details |
| A | ARG70 | |
| B | ARG70 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Increases basicity of active site His => ECO:0000255|HAMAP-Rule:MF_01292 |
| Chain | Residue | Details |
| A | ASP84 | |
| B | ASP84 |
