2FKN
crystal structure of urocanase from bacillus subtilis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006547 | biological_process | L-histidine metabolic process |
| A | 0006548 | biological_process | L-histidine catabolic process |
| A | 0016153 | molecular_function | urocanate hydratase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019556 | biological_process | L-histidine catabolic process to glutamate and formamide |
| A | 0019557 | biological_process | L-histidine catabolic process to glutamate and formate |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006547 | biological_process | L-histidine metabolic process |
| B | 0006548 | biological_process | L-histidine catabolic process |
| B | 0016153 | molecular_function | urocanate hydratase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019556 | biological_process | L-histidine catabolic process to glutamate and formamide |
| B | 0019557 | biological_process | L-histidine catabolic process to glutamate and formate |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006547 | biological_process | L-histidine metabolic process |
| C | 0006548 | biological_process | L-histidine catabolic process |
| C | 0016153 | molecular_function | urocanate hydratase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019556 | biological_process | L-histidine catabolic process to glutamate and formamide |
| C | 0019557 | biological_process | L-histidine catabolic process to glutamate and formate |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006547 | biological_process | L-histidine metabolic process |
| D | 0006548 | biological_process | L-histidine catabolic process |
| D | 0016153 | molecular_function | urocanate hydratase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0019556 | biological_process | L-histidine catabolic process to glutamate and formamide |
| D | 0019557 | biological_process | L-histidine catabolic process to glutamate and formate |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 553 |
| Chain | Residue |
| A | TYR48 |
| A | THR129 |
| A | TYR135 |
| A | GLY140 |
| A | MET174 |
| A | ARG358 |
| A | ASP439 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT B 553 |
| Chain | Residue |
| B | GLY140 |
| B | MET174 |
| B | ARG358 |
| B | ASP439 |
| B | HOH6590 |
| B | HOH6628 |
| B | TYR48 |
| B | THR129 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT C 553 |
| Chain | Residue |
| C | TYR48 |
| C | THR129 |
| C | TYR135 |
| C | GLY140 |
| C | MET174 |
| C | ARG358 |
| C | ASP439 |
| C | HOH7619 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACT D 553 |
| Chain | Residue |
| D | TYR48 |
| D | THR129 |
| D | TYR135 |
| D | GLY140 |
| D | MET174 |
| D | ARG358 |
| D | ASP439 |
| D | HOH8603 |
| D | HOH8645 |
| site_id | AC5 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD A 5555 |
| Chain | Residue |
| A | TYR48 |
| A | GLY49 |
| A | GLY50 |
| A | GLN127 |
| A | ILE141 |
| A | GLY172 |
| A | GLY173 |
| A | MET174 |
| A | GLY175 |
| A | VAL192 |
| A | GLU193 |
| A | VAL194 |
| A | ARG198 |
| A | ASN239 |
| A | ALA240 |
| A | GLN260 |
| A | THR261 |
| A | SER262 |
| A | HIS264 |
| A | GLY269 |
| A | TYR270 |
| A | VAL271 |
| A | TYR319 |
| A | ASN321 |
| A | PHE341 |
| A | LEU441 |
| A | ARG451 |
| A | GLY489 |
| A | HOH5594 |
| A | HOH5619 |
| A | HOH5621 |
| A | HOH5669 |
| A | HOH5729 |
| site_id | AC6 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD B 6555 |
| Chain | Residue |
| B | TYR48 |
| B | GLY49 |
| B | GLY50 |
| B | GLN127 |
| B | ILE141 |
| B | GLY172 |
| B | GLY173 |
| B | MET174 |
| B | GLY175 |
| B | VAL192 |
| B | GLU193 |
| B | VAL194 |
| B | ARG198 |
| B | ASN239 |
| B | ALA240 |
| B | GLN260 |
| B | THR261 |
| B | SER262 |
| B | HIS264 |
| B | GLY269 |
| B | TYR270 |
| B | VAL271 |
| B | TYR319 |
| B | ASN321 |
| B | PHE341 |
| B | LEU441 |
| B | ARG451 |
| B | GLY489 |
| B | HOH6560 |
| B | HOH6563 |
| B | HOH6653 |
| B | HOH6675 |
| site_id | AC7 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD C 7555 |
| Chain | Residue |
| C | GLY50 |
| C | GLN127 |
| C | ILE141 |
| C | GLY172 |
| C | GLY173 |
| C | MET174 |
| C | GLY175 |
| C | VAL192 |
| C | GLU193 |
| C | VAL194 |
| C | ARG198 |
| C | ASN239 |
| C | ALA240 |
| C | GLN260 |
| C | THR261 |
| C | SER262 |
| C | HIS264 |
| C | GLY269 |
| C | TYR270 |
| C | VAL271 |
| C | TYR319 |
| C | GLY320 |
| C | ASN321 |
| C | PHE341 |
| C | LEU441 |
| C | ARG451 |
| C | GLY489 |
| C | HOH7583 |
| C | HOH7602 |
| C | HOH7663 |
| C | TYR48 |
| C | GLY49 |
| site_id | AC8 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD D 8555 |
| Chain | Residue |
| D | GLU40 |
| D | TYR48 |
| D | GLY49 |
| D | GLY50 |
| D | GLN127 |
| D | ILE141 |
| D | GLY172 |
| D | GLY173 |
| D | MET174 |
| D | GLY175 |
| D | VAL192 |
| D | GLU193 |
| D | VAL194 |
| D | ARG198 |
| D | ASN239 |
| D | ALA240 |
| D | GLN260 |
| D | THR261 |
| D | SER262 |
| D | HIS264 |
| D | GLY269 |
| D | TYR270 |
| D | VAL271 |
| D | TYR319 |
| D | GLY320 |
| D | ASN321 |
| D | PHE341 |
| D | LEU441 |
| D | ARG451 |
| D | GLY489 |
| D | HOH8557 |
| D | HOH8629 |
Functional Information from PROSITE/UniProt
| site_id | PS01233 |
| Number of Residues | 16 |
| Details | UROCANASE Urocanase signature. RDHlDcGSvaSPnRET |
| Chain | Residue | Details |
| A | ARG438-THR453 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00577","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 56 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00577","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of urocanase from Bacillus subtilis.","authors":["Yu Y.-M.","Liang Y.-H.","Su X.-D."]}},{"source":"PDB","id":"2FKN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
