4B5T
Crystal structures of divalent metal dependent pyruvate aldolase, HpaI, in complex with ketobutyrate
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 | 6 |
Details | BINDING SITE FOR RESIDUE CO A 1000 |
Chain | Residue |
A | GLN147 |
A | GLU149 |
A | ASP175 |
A | HOH2117 |
A | HOH2121 |
A | 2KT4000 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GOL A 1001 |
Chain | Residue |
A | GOL1002 |
A | HOH2076 |
A | HOH2079 |
B | LEU22 |
B | SER23 |
B | GLN51 |
B | LEU54 |
B | HOH2119 |
A | SER24 |
A | SER25 |
A | TYR26 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 1002 |
Chain | Residue |
A | SER23 |
A | LEU54 |
A | GOL1001 |
A | HOH2136 |
A | HOH2150 |
A | HOH2601 |
B | SER24 |
B | SER25 |
B | HOH2066 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 1003 |
Chain | Residue |
A | GLN147 |
A | GLU149 |
A | ASP175 |
A | HOH2117 |
A | HOH2121 |
A | 2KT4000 |
site_id | AC5 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 2KT A 4000 |
Chain | Residue |
A | TRP19 |
A | ARG70 |
A | GLN147 |
A | GLU149 |
A | PHE170 |
A | GLY172 |
A | PRO173 |
A | ALA174 |
A | ASP175 |
A | LEU212 |
A | CO1000 |
A | MG1003 |
A | HOH2121 |
A | HOH2167 |
A | HOH2424 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CO B 1000 |
Chain | Residue |
B | GLN147 |
B | GLU149 |
B | ASP175 |
B | HOH2098 |
B | HOH2105 |
B | 2KT4000 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 1001 |
Chain | Residue |
B | GLN147 |
B | GLU149 |
B | ASP175 |
B | HOH2098 |
B | HOH2105 |
B | 2KT4000 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 1002 |
Chain | Residue |
A | GLU204 |
B | MET154 |
B | LEU157 |
B | GLN197 |
B | GLN201 |
B | HOH2269 |
B | HOH2309 |
B | HOH2501 |
B | HOH2502 |
site_id | AC9 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 2KT B 4000 |
Chain | Residue |
B | TRP19 |
B | ARG70 |
B | GLN147 |
B | GLU149 |
B | PHE170 |
B | GLY172 |
B | PRO173 |
B | ALA174 |
B | ASP175 |
B | LEU212 |
B | CO1000 |
B | MG1001 |
B | HOH2105 |
B | HOH2147 |
B | HOH2366 |
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 |