1JOF
Neurospora crassa 3-carboxy-cis,cis-mucoante lactonizing enzyme
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0017057 | molecular_function | 6-phosphogluconolactonase activity |
| A | 0042952 | biological_process | beta-ketoadipate pathway |
| A | 0047768 | molecular_function | carboxy-cis,cis-muconate cyclase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0017057 | molecular_function | 6-phosphogluconolactonase activity |
| B | 0042952 | biological_process | beta-ketoadipate pathway |
| B | 0047768 | molecular_function | carboxy-cis,cis-muconate cyclase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0017057 | molecular_function | 6-phosphogluconolactonase activity |
| C | 0042952 | biological_process | beta-ketoadipate pathway |
| C | 0047768 | molecular_function | carboxy-cis,cis-muconate cyclase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0017057 | molecular_function | 6-phosphogluconolactonase activity |
| D | 0042952 | biological_process | beta-ketoadipate pathway |
| D | 0047768 | molecular_function | carboxy-cis,cis-muconate cyclase activity |
| E | 0016853 | molecular_function | isomerase activity |
| E | 0017057 | molecular_function | 6-phosphogluconolactonase activity |
| E | 0042952 | biological_process | beta-ketoadipate pathway |
| E | 0047768 | molecular_function | carboxy-cis,cis-muconate cyclase activity |
| F | 0016853 | molecular_function | isomerase activity |
| F | 0017057 | molecular_function | 6-phosphogluconolactonase activity |
| F | 0042952 | biological_process | beta-ketoadipate pathway |
| F | 0047768 | molecular_function | carboxy-cis,cis-muconate cyclase activity |
| G | 0016853 | molecular_function | isomerase activity |
| G | 0017057 | molecular_function | 6-phosphogluconolactonase activity |
| G | 0042952 | biological_process | beta-ketoadipate pathway |
| G | 0047768 | molecular_function | carboxy-cis,cis-muconate cyclase activity |
| H | 0016853 | molecular_function | isomerase activity |
| H | 0017057 | molecular_function | 6-phosphogluconolactonase activity |
| H | 0042952 | biological_process | beta-ketoadipate pathway |
| H | 0047768 | molecular_function | carboxy-cis,cis-muconate cyclase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 366 |
| Chain | Residue |
| A | ARG216 |
| A | TYR231 |
| A | HOH1081 |
| A | HOH1367 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 366 |
| Chain | Residue |
| B | PRO189 |
| B | ARG216 |
| B | TYR231 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 366 |
| Chain | Residue |
| C | HOH1547 |
| C | ARG216 |
| C | TYR231 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 461 |
| Chain | Residue |
| D | PRO189 |
| D | ARG216 |
| D | TYR231 |
| D | HOH1082 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 E 561 |
| Chain | Residue |
| E | ARG216 |
| E | TYR231 |
| E | HOH1083 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 F 661 |
| Chain | Residue |
| F | PRO189 |
| F | ARG216 |
| F | TYR231 |
| F | HOH1084 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 G 761 |
| Chain | Residue |
| G | ARG216 |
| G | TYR231 |
| G | HOH1283 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 H 861 |
| Chain | Residue |
| H | PRO189 |
| H | ARG216 |
| H | TYR231 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PIN B 9012 |
| Chain | Residue |
| A | ARG349 |
| B | GLU279 |
| B | PRO305 |
| B | GLU331 |
| B | TRP333 |
| B | ARG349 |
| C | GLU35 |
| C | PRO37 |
| C | GLN38 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PIN H 9078 |
| Chain | Residue |
| F | ARG86 |
| F | PHE117 |
| G | ARG349 |
| H | PHE278 |
| H | GLU279 |
| H | PRO305 |
| H | GLU331 |
| H | TRP333 |
| H | ARG349 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME A 367 |
| Chain | Residue |
| A | ARG290 |
| A | CYS292 |
| E | ALA176 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME A 368 |
| Chain | Residue |
| A | HIS3 |
| A | CYS317 |
| A | TRP319 |
| A | TRP363 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME B 9013 |
| Chain | Residue |
| B | ARG290 |
| B | CYS292 |
| F | ALA176 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME B 9014 |
| Chain | Residue |
| B | HIS3 |
| B | CYS317 |
| B | TRP319 |
| B | TRP363 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME C 367 |
| Chain | Residue |
| C | ARG290 |
| C | CYS292 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME C 399 |
| Chain | Residue |
| C | HIS3 |
| C | CYS317 |
| C | TRP319 |
| C | TRP363 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME D 466 |
| Chain | Residue |
| D | ARG290 |
| D | CYS292 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME D 499 |
| Chain | Residue |
| D | HIS3 |
| D | CYS317 |
| D | TRP319 |
| D | TRP363 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME E 566 |
| Chain | Residue |
| E | ARG290 |
| E | CYS292 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME E 599 |
| Chain | Residue |
| E | HIS3 |
| E | CYS317 |
| E | TRP319 |
| E | TRP363 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME F 666 |
| Chain | Residue |
| B | ALA176 |
| F | ARG290 |
| F | CYS292 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME F 699 |
| Chain | Residue |
| F | HIS3 |
| F | CYS317 |
| F | TRP319 |
| F | TRP363 |
| site_id | CC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME G 766 |
| Chain | Residue |
| G | ARG290 |
| G | CYS292 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME G 799 |
| Chain | Residue |
| G | HIS3 |
| G | CYS317 |
| G | TRP319 |
| G | TRP363 |
| site_id | CC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME H 1866 |
| Chain | Residue |
| H | ARG290 |
| H | CYS292 |
| site_id | CC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME H 1899 |
| Chain | Residue |
| H | HIS3 |
| H | CYS317 |
| H | TRP319 |
| H | TRP363 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | GLY149 | |
| C | TRP197 | |
| C | ALA213 | |
| C | ALA275 | |
| D | GLY149 | |
| D | TRP197 | |
| D | ALA213 | |
| D | ALA275 | |
| E | GLY149 | |
| E | TRP197 | |
| E | ALA213 | |
| A | TRP197 | |
| E | ALA275 | |
| F | GLY149 | |
| F | TRP197 | |
| F | ALA213 | |
| F | ALA275 | |
| G | GLY149 | |
| G | TRP197 | |
| G | ALA213 | |
| G | ALA275 | |
| H | GLY149 | |
| A | ALA213 | |
| H | TRP197 | |
| H | ALA213 | |
| H | ALA275 | |
| A | ALA275 | |
| B | GLY149 | |
| B | TRP197 | |
| B | ALA213 | |
| B | ALA275 | |
| C | GLY149 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 11937053 |
| Chain | Residue | Details |
| A | GLU212 | |
| A | HIS148 | |
| A | ARG274 | |
| A | ARG196 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 11937053 |
| Chain | Residue | Details |
| B | GLU212 | |
| B | HIS148 | |
| B | ARG274 | |
| B | ARG196 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 11937053 |
| Chain | Residue | Details |
| C | GLU212 | |
| C | HIS148 | |
| C | ARG274 | |
| C | ARG196 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 11937053 |
| Chain | Residue | Details |
| D | GLU212 | |
| D | HIS148 | |
| D | ARG274 | |
| D | ARG196 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 11937053 |
| Chain | Residue | Details |
| E | GLU212 | |
| E | HIS148 | |
| E | ARG274 | |
| E | ARG196 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 11937053 |
| Chain | Residue | Details |
| F | GLU212 | |
| F | HIS148 | |
| F | ARG274 | |
| F | ARG196 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 11937053 |
| Chain | Residue | Details |
| G | GLU212 | |
| G | HIS148 | |
| G | ARG274 | |
| G | ARG196 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 11937053 |
| Chain | Residue | Details |
| H | GLU212 | |
| H | HIS148 | |
| H | ARG274 | |
| H | ARG196 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 542 |
| Chain | Residue | Details |
| A | TYR160 | proton acceptor |
| A | GLU212 | electrostatic stabiliser, increase nucleophilicity |
| A | PHE236 | proton donor |
| A | THR306 | electrostatic stabiliser, increase nucleophilicity |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 542 |
| Chain | Residue | Details |
| B | TYR160 | proton acceptor |
| B | GLU212 | electrostatic stabiliser, increase nucleophilicity |
| B | PHE236 | proton donor |
| B | THR306 | electrostatic stabiliser, increase nucleophilicity |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 542 |
| Chain | Residue | Details |
| C | TYR160 | proton acceptor |
| C | GLU212 | electrostatic stabiliser, increase nucleophilicity |
| C | PHE236 | proton donor |
| C | THR306 | electrostatic stabiliser, increase nucleophilicity |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 542 |
| Chain | Residue | Details |
| D | TYR160 | proton acceptor |
| D | GLU212 | electrostatic stabiliser, increase nucleophilicity |
| D | PHE236 | proton donor |
| D | THR306 | electrostatic stabiliser, increase nucleophilicity |
| site_id | MCSA5 |
| Number of Residues | 4 |
| Details | M-CSA 542 |
| Chain | Residue | Details |
| E | TYR160 | proton acceptor |
| E | GLU212 | electrostatic stabiliser, increase nucleophilicity |
| E | PHE236 | proton donor |
| E | THR306 | electrostatic stabiliser, increase nucleophilicity |
| site_id | MCSA6 |
| Number of Residues | 4 |
| Details | M-CSA 542 |
| Chain | Residue | Details |
| F | TYR160 | proton acceptor |
| F | GLU212 | electrostatic stabiliser, increase nucleophilicity |
| F | PHE236 | proton donor |
| F | THR306 | electrostatic stabiliser, increase nucleophilicity |
| site_id | MCSA7 |
| Number of Residues | 4 |
| Details | M-CSA 542 |
| Chain | Residue | Details |
| G | TYR160 | proton acceptor |
| G | GLU212 | electrostatic stabiliser, increase nucleophilicity |
| G | PHE236 | proton donor |
| G | THR306 | electrostatic stabiliser, increase nucleophilicity |
| site_id | MCSA8 |
| Number of Residues | 4 |
| Details | M-CSA 542 |
| Chain | Residue | Details |
| H | TYR160 | proton acceptor |
| H | GLU212 | electrostatic stabiliser, increase nucleophilicity |
| H | PHE236 | proton donor |
| H | THR306 | electrostatic stabiliser, increase nucleophilicity |
