4EAY
Crystal structures of mannonate dehydratase from Escherichia coli strain K12 complexed with D-mannonate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006064 | biological_process | glucuronate catabolic process |
| A | 0006974 | biological_process | DNA damage response |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0008927 | molecular_function | mannonate dehydratase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0042840 | biological_process | D-glucuronate catabolic process |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006064 | biological_process | glucuronate catabolic process |
| B | 0006974 | biological_process | DNA damage response |
| B | 0008198 | molecular_function | ferrous iron binding |
| B | 0008927 | molecular_function | mannonate dehydratase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0042840 | biological_process | D-glucuronate catabolic process |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0006064 | biological_process | glucuronate catabolic process |
| C | 0006974 | biological_process | DNA damage response |
| C | 0008198 | molecular_function | ferrous iron binding |
| C | 0008927 | molecular_function | mannonate dehydratase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0030145 | molecular_function | manganese ion binding |
| C | 0042840 | biological_process | D-glucuronate catabolic process |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0006064 | biological_process | glucuronate catabolic process |
| D | 0006974 | biological_process | DNA damage response |
| D | 0008198 | molecular_function | ferrous iron binding |
| D | 0008927 | molecular_function | mannonate dehydratase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0030145 | molecular_function | manganese ion binding |
| D | 0042840 | biological_process | D-glucuronate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 401 |
| Chain | Residue |
| A | ARG6 |
| A | ARG349 |
| A | PRO350 |
| A | ASP351 |
| A | ARG373 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE CS2 A 402 |
| Chain | Residue |
| A | TRP110 |
| A | HIS233 |
| A | ASP236 |
| A | CYS271 |
| A | SER274 |
| A | HIS298 |
| A | ARG300 |
| A | ARG349 |
| A | ASP351 |
| A | HIS352 |
| A | TYR368 |
| A | MN403 |
| A | HOH566 |
| A | HOH586 |
| A | ARG6 |
| A | GLU63 |
| A | ASN103 |
| A | ASP109 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 403 |
| Chain | Residue |
| A | HIS233 |
| A | CYS271 |
| A | HIS298 |
| A | ASP351 |
| A | CS2402 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 401 |
| Chain | Residue |
| B | ARG6 |
| B | ARG349 |
| B | PRO350 |
| B | ASP351 |
| B | ARG373 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE CS2 B 402 |
| Chain | Residue |
| B | ARG6 |
| B | GLU63 |
| B | ASN103 |
| B | ASP109 |
| B | TRP110 |
| B | HIS233 |
| B | ASP236 |
| B | CYS271 |
| B | SER274 |
| B | HIS298 |
| B | ARG300 |
| B | ARG349 |
| B | ASP351 |
| B | HIS352 |
| B | TYR368 |
| B | MN403 |
| B | HOH518 |
| B | HOH719 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 403 |
| Chain | Residue |
| B | HIS233 |
| B | CYS271 |
| B | HIS298 |
| B | ASP351 |
| B | CS2402 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL C 401 |
| Chain | Residue |
| C | ARG6 |
| C | ARG349 |
| C | PRO350 |
| C | ASP351 |
| C | ARG373 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN C 402 |
| Chain | Residue |
| C | HIS233 |
| C | CYS271 |
| C | HIS298 |
| C | ASP351 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL D 401 |
| Chain | Residue |
| D | ARG6 |
| D | ARG349 |
| D | PRO350 |
| D | ASP351 |
| D | ARG373 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN D 402 |
| Chain | Residue |
| D | HIS233 |
| D | CYS271 |
| D | HIS298 |
| D | ASP351 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 963 |
| Chain | Residue | Details |
| A | HIS233 | metal ligand |
| A | CYS271 | metal ligand |
| A | HIS298 | metal ligand |
| A | ASP351 | metal ligand |
| A | HIS352 | proton acceptor, proton donor |
| A | TYR368 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 963 |
| Chain | Residue | Details |
| B | HIS233 | metal ligand |
| B | CYS271 | metal ligand |
| B | HIS298 | metal ligand |
| B | ASP351 | metal ligand |
| B | HIS352 | proton acceptor, proton donor |
| B | TYR368 | proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 963 |
| Chain | Residue | Details |
| C | HIS233 | metal ligand |
| C | CYS271 | metal ligand |
| C | HIS298 | metal ligand |
| C | ASP351 | metal ligand |
| C | HIS352 | proton acceptor, proton donor |
| C | TYR368 | proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 6 |
| Details | M-CSA 963 |
| Chain | Residue | Details |
| D | HIS233 | metal ligand |
| D | CYS271 | metal ligand |
| D | HIS298 | metal ligand |
| D | ASP351 | metal ligand |
| D | HIS352 | proton acceptor, proton donor |
| D | TYR368 | proton acceptor, proton donor |
