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 |