1X87
2.4A X-ray structure of Urocanase protein complexed with NAD
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAD A 600 |
| Chain | Residue |
| A | GLY171 |
| A | GLN259 |
| A | THR260 |
| A | SER261 |
| A | HIS263 |
| A | GLY268 |
| A | TYR269 |
| A | ILE270 |
| A | TYR318 |
| A | GLY319 |
| A | ASN320 |
| A | GLY172 |
| A | PHE340 |
| A | HOH621 |
| A | HOH627 |
| A | MSE173 |
| A | GLY174 |
| A | GLU192 |
| A | VAL193 |
| A | ARG197 |
| A | ASN238 |
| A | ALA239 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAD B 600 |
| Chain | Residue |
| B | GLY169 |
| B | GLY171 |
| B | GLY172 |
| B | MSE173 |
| B | GLY174 |
| B | GLU192 |
| B | VAL193 |
| B | ARG197 |
| B | ASN238 |
| B | ALA239 |
| B | GLN259 |
| B | THR260 |
| B | HIS263 |
| B | GLY268 |
| B | TYR269 |
| B | ILE270 |
| B | TYR318 |
| B | ASN320 |
| B | PHE340 |
| B | HOH815 |
Functional Information from PROSITE/UniProt
| site_id | PS01233 |
| Number of Residues | 16 |
| Details | UROCANASE Urocanase signature. RDHlDsGSvaSPnRET |
| Chain | Residue | Details |
| A | ARG437-THR452 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00577","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00577","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2004","submissionDatabase":"PDB data bank","title":"2.4A x-ray structure of urocanase protein complexed with NAD.","authors":["Tereshko V.","Zaborske J.","Gilbreth R.","Dementieva I.","Collart F.","Joachimiak A.","Kossiakoff A."]}},{"source":"PDB","id":"1X87","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
