2V7G
Crystal Structure of an Engineered Urocanase Tetramer
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 | 36 |
| Details | BINDING SITE FOR RESIDUE NAD A 3001 |
| Chain | Residue |
| A | GLU44 |
| A | GLY179 |
| A | GLU197 |
| A | SER198 |
| A | GLN199 |
| A | ARG202 |
| A | GLY242 |
| A | ASN243 |
| A | ALA244 |
| A | GLN264 |
| A | THR265 |
| A | TYR52 |
| A | SER266 |
| A | HIS268 |
| A | GLY273 |
| A | TYR274 |
| A | LEU275 |
| A | TRP281 |
| A | TYR323 |
| A | GLY324 |
| A | ASN325 |
| A | PHE345 |
| A | GLY53 |
| A | LEU445 |
| A | ARG455 |
| A | GLY493 |
| A | HOH2344 |
| A | HOH2345 |
| A | HOH2346 |
| A | HOH2347 |
| A | GLY54 |
| A | GLN131 |
| A | ILE145 |
| A | GLY176 |
| A | GLY177 |
| A | MET178 |
| site_id | AC2 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NAD B 3001 |
| Chain | Residue |
| B | GLU44 |
| B | TYR52 |
| B | GLY53 |
| B | GLY54 |
| B | GLN131 |
| B | ILE145 |
| B | GLY176 |
| B | GLY177 |
| B | MET178 |
| B | GLY179 |
| B | GLU197 |
| B | SER198 |
| B | GLN199 |
| B | ARG202 |
| B | GLY242 |
| B | ASN243 |
| B | ALA244 |
| B | GLN264 |
| B | THR265 |
| B | SER266 |
| B | HIS268 |
| B | GLY273 |
| B | TYR274 |
| B | LEU275 |
| B | TRP281 |
| B | TYR323 |
| B | GLY324 |
| B | ASN325 |
| B | PHE345 |
| B | LEU445 |
| B | ARG455 |
| B | GLY493 |
| B | HOH2035 |
| B | HOH2192 |
| B | HOH2340 |
| B | HOH2341 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD C 3001 |
| Chain | Residue |
| C | HOH2329 |
| C | HOH2330 |
| C | GLY176 |
| C | GLY177 |
| C | MET178 |
| C | GLY179 |
| C | GLU197 |
| C | SER198 |
| C | GLN199 |
| C | ARG202 |
| C | GLY242 |
| C | ASN243 |
| C | ALA244 |
| C | GLN264 |
| C | THR265 |
| C | SER266 |
| C | HIS268 |
| C | GLY273 |
| C | TYR274 |
| C | LEU275 |
| C | TRP281 |
| C | TYR323 |
| C | GLY324 |
| C | ASN325 |
| C | PHE345 |
| C | ARG455 |
| C | ACT1558 |
| C | HOH2180 |
| C | HOH2275 |
| site_id | AC4 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD D 3001 |
| Chain | Residue |
| D | GLY176 |
| D | GLY177 |
| D | MET178 |
| D | GLY179 |
| D | GLU197 |
| D | SER198 |
| D | GLN199 |
| D | ARG202 |
| D | GLY242 |
| D | ASN243 |
| D | ALA244 |
| D | GLN264 |
| D | THR265 |
| D | SER266 |
| D | HIS268 |
| D | GLY273 |
| D | TYR274 |
| D | LEU275 |
| D | TYR323 |
| D | GLY324 |
| D | ASN325 |
| D | PHE345 |
| D | ARG455 |
| D | HOH2241 |
| D | HOH2287 |
| D | HOH2288 |
| D | HOH2289 |
| D | HOH2290 |
| D | HOH2291 |
| D | HOH2292 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT C 1558 |
| Chain | Residue |
| C | HIS268 |
| C | GLY324 |
| C | ARG455 |
| C | NAD3001 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 1558 |
| Chain | Residue |
| B | LYS87 |
| B | HOH2332 |
| B | HOH2333 |
| D | ASP535 |
| D | MET554 |
| D | ILE555 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 1559 |
| Chain | Residue |
| B | VAL91 |
| B | HOH2334 |
| B | HOH2335 |
| D | ASP551 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ACT A 1558 |
| Chain | Residue |
| A | TYR52 |
| A | THR133 |
| A | TYR139 |
| A | GLY144 |
| A | ILE145 |
| A | MET178 |
| A | ARG362 |
| A | ASP443 |
| A | HOH2127 |
| A | HOH2291 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ACT B 1560 |
| Chain | Residue |
| B | TYR52 |
| B | THR133 |
| B | TYR139 |
| B | GLY144 |
| B | ILE145 |
| B | MET178 |
| B | ARG362 |
| B | ASP443 |
| B | HOH2275 |
| B | HOH2336 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 1559 |
| Chain | Residue |
| A | GLN199 |
| A | HOH2342 |
| A | HOH2343 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT C 1559 |
| Chain | Residue |
| C | TYR52 |
| C | THR133 |
| C | TYR139 |
| C | GLY144 |
| C | ARG362 |
| C | HOH2112 |
| C | HOH2326 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 1561 |
| Chain | Residue |
| B | PRO453 |
| B | ASN454 |
| B | ASP465 |
| B | HOH2220 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 1558 |
| Chain | Residue |
| D | SER198 |
| D | GLY242 |
| D | ASN243 |
| D | LEU275 |
| D | THR280 |
| D | TRP281 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1562 |
| Chain | Residue |
| B | GLU151 |
| B | ARG158 |
| B | HIS389 |
| B | HOH2337 |
| B | HOH2338 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL D 1559 |
| Chain | Residue |
| A | HOH2202 |
| D | GLU246 |
| D | GLY278 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1560 |
| Chain | Residue |
| A | ILE277 |
| A | TRP279 |
| A | ALA298 |
| A | SER302 |
| D | PRO276 |
| D | ILE277 |
| D | TRP279 |
| D | SER302 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 1560 |
| Chain | Residue |
| D | SER198 |
| D | GLN200 |
| D | SER201 |
| D | HIS241 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1563 |
| Chain | Residue |
| B | HIS160 |
| B | GLN314 |
| B | THR320 |
| B | PRO343 |
| B | TYR349 |
| B | HOH2339 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1561 |
| Chain | Residue |
| A | ARG356 |
| A | ASP387 |
| A | TRP412 |
| A | LEU417 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 1561 |
| Chain | Residue |
| D | GLU151 |
| D | ARG158 |
| D | LEU390 |
| D | TRP412 |
Functional Information from PROSITE/UniProt
| site_id | PS01233 |
| Number of Residues | 16 |
| Details | UROCANASE Urocanase signature. RDHlDsGSvsSPnRET |
| Chain | Residue | Details |
| A | ARG442-THR457 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00577, ECO:0000305|PubMed:7901006 |
| Chain | Residue | Details |
| A | TRP412 | |
| B | TRP412 | |
| C | TRP412 | |
| D | TRP412 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00577, ECO:0000269|PubMed:15313616, ECO:0000269|PubMed:18187656, ECO:0007744|PDB:1UWK, ECO:0007744|PDB:1UWL, ECO:0007744|PDB:1W1U, ECO:0007744|PDB:2V7G |
| Chain | Residue | Details |
| A | GLY54 | |
| B | MET178 | |
| B | ALA244 | |
| B | THR265 | |
| B | LEU275 | |
| B | VAL494 | |
| C | GLY54 | |
| C | MET132 | |
| C | MET178 | |
| C | ALA244 | |
| C | THR265 | |
| A | MET132 | |
| C | LEU275 | |
| C | VAL494 | |
| D | GLY54 | |
| D | MET132 | |
| D | MET178 | |
| D | ALA244 | |
| D | THR265 | |
| D | LEU275 | |
| D | VAL494 | |
| A | MET178 | |
| A | ALA244 | |
| A | THR265 | |
| A | LEU275 | |
| A | VAL494 | |
| B | GLY54 | |
| B | MET132 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15313616, ECO:0000269|PubMed:18187656, ECO:0007744|PDB:1UWK, ECO:0007744|PDB:1UWL, ECO:0007744|PDB:1W1U, ECO:0007744|PDB:2V7G |
| Chain | Residue | Details |
| A | SER198 | |
| B | SER198 | |
| C | SER198 | |
| D | SER198 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15313616, ECO:0000269|PubMed:18187656, ECO:0007744|PDB:1UWK, ECO:0007744|PDB:1UWL, ECO:0007744|PDB:2V7G |
| Chain | Residue | Details |
| A | GLY324 | |
| B | GLY324 | |
| C | GLY324 | |
| D | GLY324 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15313616, ECO:0000269|PubMed:18187656, ECO:0007744|PDB:1W1U, ECO:0007744|PDB:2V7G |
| Chain | Residue | Details |
| A | GLU456 | |
| B | GLU456 | |
| C | GLU456 | |
| D | GLU456 |
