4B5S
Crystal structures of divalent metal dependent pyruvate aldolase, HpaI, in complex with pyruvate
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 | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 1252 |
| Chain | Residue |
| A | LEU22 |
| B | HOH2497 |
| A | SER23 |
| A | PRO47 |
| A | 3GR1252 |
| A | HOH2147 |
| B | SER24 |
| B | TYR26 |
| B | HOH2093 |
| B | HOH2095 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 3GR A 1252 |
| Chain | Residue |
| A | SER24 |
| A | TYR26 |
| A | HOH2092 |
| A | HOH2096 |
| A | HOH2525 |
| B | LEU22 |
| B | SER23 |
| B | PRO47 |
| B | GLN51 |
| B | LEU54 |
| B | GOL1252 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO A 1253 |
| Chain | Residue |
| A | GLN147 |
| A | GLU149 |
| A | ASP175 |
| A | PYR1256 |
| A | HOH2140 |
| A | HOH2144 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1254 |
| Chain | Residue |
| A | VAL118 |
| A | SER120 |
| A | ALA121 |
| A | ASN129 |
| A | ALA174 |
| A | HOH2431 |
| A | HOH2434 |
| A | HOH2526 |
| A | HOH2527 |
| A | HOH2529 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1255 |
| Chain | Residue |
| A | LYS10 |
| A | ALA11 |
| A | GLY12 |
| A | ARG203 |
| A | HOH2043 |
| A | HOH2463 |
| A | HOH2472 |
| A | HOH2530 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PYR A 1256 |
| Chain | Residue |
| A | ARG70 |
| A | GLN147 |
| A | GLU149 |
| A | PHE170 |
| A | GLY172 |
| A | PRO173 |
| A | ALA174 |
| A | ASP175 |
| A | LEU212 |
| A | CO1253 |
| A | MG1257 |
| A | HOH2144 |
| A | HOH2210 |
| A | HOH2528 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1257 |
| Chain | Residue |
| A | GLN147 |
| A | GLU149 |
| A | ASP175 |
| A | PYR1256 |
| A | HOH2140 |
| A | HOH2144 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO B 1253 |
| Chain | Residue |
| B | GLN147 |
| B | GLU149 |
| B | ASP175 |
| B | PYR1256 |
| B | HOH2143 |
| B | HOH2149 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1254 |
| Chain | Residue |
| B | VAL118 |
| B | GLY119 |
| B | SER120 |
| B | ALA121 |
| B | ASN129 |
| B | ALA174 |
| B | HOH2409 |
| B | HOH2410 |
| B | HOH2499 |
| B | HOH2500 |
| B | HOH2503 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1255 |
| Chain | Residue |
| B | GLY12 |
| B | ARG203 |
| B | HOH2051 |
| B | HOH2437 |
| site_id | BC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PYR B 1256 |
| Chain | Residue |
| B | HOH2502 |
| B | ARG70 |
| B | GLN147 |
| B | GLU149 |
| B | PHE170 |
| B | GLY172 |
| B | PRO173 |
| B | ALA174 |
| B | ASP175 |
| B | LEU212 |
| B | CO1253 |
| B | MG1257 |
| B | HOH2149 |
| B | HOH2215 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1257 |
| Chain | Residue |
| B | GLN147 |
| B | GLU149 |
| B | ASP175 |
| B | PYR1256 |
| B | HOH2143 |
| B | HOH2149 |
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 |
