4B5V
Crystal structures of divalent metal dependent pyruvate aldolase, HpaI, in complex with 4-hydroxyl-2-ketoheptane-1,7-dioate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0009056 | biological_process | catabolic process |
| 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 | 0043863 | molecular_function | 4-hydroxy-2-ketopimelate aldolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0009056 | biological_process | catabolic process |
| 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 | 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 | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 1252 |
| Chain | Residue |
| A | LEU22 |
| A | SER23 |
| A | LEU54 |
| A | HOH2130 |
| A | HOH2136 |
| A | HOH2146 |
| B | SER24 |
| B | TYR26 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PYR B 1253 |
| Chain | Residue |
| B | GLN147 |
| B | GLU149 |
| B | PHE170 |
| B | GLY172 |
| B | PRO173 |
| B | ALA174 |
| B | ASP175 |
| B | LEU212 |
| B | MG1255 |
| B | HOH2157 |
| B | HOH2383 |
| B | HOH2384 |
| B | ARG70 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE E8U B 1254 |
| Chain | Residue |
| B | HIS45 |
| B | ARG70 |
| B | VAL118 |
| B | GLY119 |
| B | SER120 |
| B | ALA121 |
| B | GLN147 |
| B | GLY172 |
| B | PRO173 |
| B | ALA174 |
| B | ASP175 |
| B | LEU212 |
| B | MG1255 |
| B | HOH2121 |
| B | HOH2157 |
| B | HOH2383 |
| B | HOH2384 |
| B | HOH2385 |
| B | HOH2386 |
| B | HOH2387 |
| B | HOH2389 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PYR A 1252 |
| Chain | Residue |
| A | ARG70 |
| A | GLN147 |
| A | PHE170 |
| A | GLY172 |
| A | PRO173 |
| A | ALA174 |
| A | ASP175 |
| A | LEU212 |
| A | MG1255 |
| A | HOH2163 |
| A | HOH2403 |
| A | HOH2404 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE E8U A 1253 |
| Chain | Residue |
| A | HIS45 |
| A | ARG70 |
| A | VAL118 |
| A | GLY119 |
| A | SER120 |
| A | GLN147 |
| A | GLY172 |
| A | PRO173 |
| A | ALA174 |
| A | ASP175 |
| A | LEU212 |
| A | MG1255 |
| A | HOH2128 |
| A | HOH2163 |
| A | HOH2403 |
| A | HOH2404 |
| A | HOH2405 |
| A | HOH2406 |
| A | HOH2407 |
| A | HOH2408 |
| A | HOH2409 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1254 |
| Chain | Residue |
| A | SER24 |
| A | TYR26 |
| A | HOH2082 |
| A | HOH2410 |
| B | LEU22 |
| B | SER23 |
| B | GLN51 |
| B | LEU54 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 1255 |
| Chain | Residue |
| A | GLN147 |
| A | GLU149 |
| A | ASP175 |
| A | PYR1252 |
| A | E8U1253 |
| A | HOH2123 |
| A | HOH2128 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 1255 |
| Chain | Residue |
| B | GLN147 |
| B | GLU149 |
| B | ASP175 |
| B | PYR1253 |
| B | E8U1254 |
| B | HOH2113 |
| B | HOH2121 |
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 |
