1H5Q
Mannitol dehydrogenase from Agaricus bisporus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0019594 | biological_process | mannitol metabolic process |
| A | 0050085 | molecular_function | mannitol 2-dehydrogenase (NADP+) activity |
| A | 0050661 | molecular_function | NADP binding |
| A | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| A | 0051289 | biological_process | protein homotetramerization |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0019594 | biological_process | mannitol metabolic process |
| B | 0050085 | molecular_function | mannitol 2-dehydrogenase (NADP+) activity |
| B | 0050661 | molecular_function | NADP binding |
| B | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| B | 0051289 | biological_process | protein homotetramerization |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0019594 | biological_process | mannitol metabolic process |
| C | 0050085 | molecular_function | mannitol 2-dehydrogenase (NADP+) activity |
| C | 0050661 | molecular_function | NADP binding |
| C | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| C | 0051289 | biological_process | protein homotetramerization |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0019594 | biological_process | mannitol metabolic process |
| D | 0050085 | molecular_function | mannitol 2-dehydrogenase (NADP+) activity |
| D | 0050661 | molecular_function | NADP binding |
| D | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| D | 0051289 | biological_process | protein homotetramerization |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| E | 0019594 | biological_process | mannitol metabolic process |
| E | 0050085 | molecular_function | mannitol 2-dehydrogenase (NADP+) activity |
| E | 0050661 | molecular_function | NADP binding |
| E | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| E | 0051289 | biological_process | protein homotetramerization |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| F | 0019594 | biological_process | mannitol metabolic process |
| F | 0050085 | molecular_function | mannitol 2-dehydrogenase (NADP+) activity |
| F | 0050661 | molecular_function | NADP binding |
| F | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| F | 0051289 | biological_process | protein homotetramerization |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| G | 0019594 | biological_process | mannitol metabolic process |
| G | 0050085 | molecular_function | mannitol 2-dehydrogenase (NADP+) activity |
| G | 0050661 | molecular_function | NADP binding |
| G | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| G | 0051289 | biological_process | protein homotetramerization |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| H | 0019594 | biological_process | mannitol metabolic process |
| H | 0050085 | molecular_function | mannitol 2-dehydrogenase (NADP+) activity |
| H | 0050661 | molecular_function | NADP binding |
| H | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| H | 0051289 | biological_process | protein homotetramerization |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| I | 0019594 | biological_process | mannitol metabolic process |
| I | 0050085 | molecular_function | mannitol 2-dehydrogenase (NADP+) activity |
| I | 0050661 | molecular_function | NADP binding |
| I | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| I | 0051289 | biological_process | protein homotetramerization |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| J | 0019594 | biological_process | mannitol metabolic process |
| J | 0050085 | molecular_function | mannitol 2-dehydrogenase (NADP+) activity |
| J | 0050661 | molecular_function | NADP binding |
| J | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| J | 0051289 | biological_process | protein homotetramerization |
| K | 0016491 | molecular_function | oxidoreductase activity |
| K | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| K | 0019594 | biological_process | mannitol metabolic process |
| K | 0050085 | molecular_function | mannitol 2-dehydrogenase (NADP+) activity |
| K | 0050661 | molecular_function | NADP binding |
| K | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| K | 0051289 | biological_process | protein homotetramerization |
| L | 0016491 | molecular_function | oxidoreductase activity |
| L | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| L | 0019594 | biological_process | mannitol metabolic process |
| L | 0050085 | molecular_function | mannitol 2-dehydrogenase (NADP+) activity |
| L | 0050661 | molecular_function | NADP binding |
| L | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| L | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI A2263 |
| Chain | Residue |
| A | TRP262 |
| A | HOH2125 |
| A | HOH2127 |
| C | TRP262 |
| C | HOH2241 |
| C | HOH2243 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI B2263 |
| Chain | Residue |
| D | TRP262 |
| D | HOH2183 |
| D | HOH2184 |
| B | TRP262 |
| B | HOH2193 |
| B | HOH2195 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI E3263 |
| Chain | Residue |
| E | TRP262 |
| E | HOH2329 |
| E | HOH2333 |
| G | TRP262 |
| G | HOH2278 |
| G | HOH2281 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI F3263 |
| Chain | Residue |
| F | TRP262 |
| F | HOH2304 |
| F | HOH2306 |
| H | TRP262 |
| H | HOH2290 |
| H | HOH2291 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI I3263 |
| Chain | Residue |
| I | TRP262 |
| I | HOH2299 |
| I | HOH2300 |
| K | TRP262 |
| K | HOH2273 |
| K | HOH2275 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI J3263 |
| Chain | Residue |
| J | TRP262 |
| J | HOH2257 |
| J | HOH2260 |
| L | TRP262 |
| L | HOH2295 |
| L | HOH2297 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAP A 263 |
| Chain | Residue |
| A | ASN20 |
| A | ARG21 |
| A | GLY22 |
| A | ILE23 |
| A | TYR42 |
| A | ARG43 |
| A | SER44 |
| A | ALA45 |
| A | CYS68 |
| A | ASP69 |
| A | VAL70 |
| A | ASN96 |
| A | ALA97 |
| A | GLY98 |
| A | VAL99 |
| A | VAL119 |
| A | SER148 |
| A | SER149 |
| A | TYR169 |
| A | LYS173 |
| A | GLY200 |
| A | VAL202 |
| A | GLN206 |
| A | HOH2128 |
| A | HOH2129 |
| A | HOH2130 |
| site_id | AC8 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAP B 263 |
| Chain | Residue |
| B | GLY18 |
| B | ASN20 |
| B | ARG21 |
| B | GLY22 |
| B | ILE23 |
| B | TYR42 |
| B | ARG43 |
| B | SER44 |
| B | ALA45 |
| B | CYS68 |
| B | ASP69 |
| B | VAL70 |
| B | ASN96 |
| B | ALA97 |
| B | GLY98 |
| B | THR147 |
| B | SER148 |
| B | SER149 |
| B | TYR169 |
| B | LYS173 |
| B | PRO199 |
| B | GLY200 |
| B | VAL202 |
| B | THR204 |
| B | GLN206 |
| B | THR207 |
| B | HOH2030 |
| B | HOH2033 |
| B | HOH2087 |
| B | HOH2197 |
| B | HOH2198 |
| B | HOH2199 |
| B | HOH2200 |
| B | HOH2201 |
| site_id | AC9 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAP C 263 |
| Chain | Residue |
| C | ILE23 |
| C | TYR42 |
| C | ARG43 |
| C | SER44 |
| C | ALA45 |
| C | CYS68 |
| C | ASP69 |
| C | VAL70 |
| C | ASN96 |
| C | ALA97 |
| C | GLY98 |
| C | THR147 |
| C | SER148 |
| C | TYR169 |
| C | LYS173 |
| C | PRO199 |
| C | GLY200 |
| C | VAL202 |
| C | GLN206 |
| C | HOH2047 |
| C | HOH2114 |
| C | HOH2197 |
| C | HOH2246 |
| C | HOH2247 |
| C | HOH2248 |
| C | HOH2249 |
| C | HOH2250 |
| C | ASN20 |
| C | ARG21 |
| C | GLY22 |
| site_id | BC1 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAP D 263 |
| Chain | Residue |
| D | GLY18 |
| D | ASN20 |
| D | ARG21 |
| D | GLY22 |
| D | ILE23 |
| D | TYR42 |
| D | ARG43 |
| D | SER44 |
| D | ALA45 |
| D | CYS68 |
| D | ASP69 |
| D | VAL70 |
| D | ASN96 |
| D | ALA97 |
| D | GLY98 |
| D | VAL99 |
| D | VAL119 |
| D | THR147 |
| D | SER148 |
| D | SER149 |
| D | TYR169 |
| D | LYS173 |
| D | PRO199 |
| D | GLY200 |
| D | VAL202 |
| D | GLN206 |
| D | HOH2026 |
| D | HOH2140 |
| D | HOH2144 |
| D | HOH2186 |
| D | HOH2187 |
| D | HOH2188 |
| D | HOH2189 |
| D | HOH2190 |
| site_id | BC2 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NAP E 263 |
| Chain | Residue |
| E | GLY18 |
| E | ASN20 |
| E | ARG21 |
| E | GLY22 |
| E | ILE23 |
| E | TYR42 |
| E | ARG43 |
| E | SER44 |
| E | ALA45 |
| E | CYS68 |
| E | ASP69 |
| E | VAL70 |
| E | ASN96 |
| E | ALA97 |
| E | GLY98 |
| E | VAL119 |
| E | THR147 |
| E | SER148 |
| E | SER149 |
| E | TYR169 |
| E | LYS173 |
| E | PRO199 |
| E | GLY200 |
| E | VAL202 |
| E | GLN206 |
| E | HOH2072 |
| E | HOH2077 |
| E | HOH2271 |
| E | HOH2334 |
| E | HOH2335 |
| E | HOH2336 |
| E | HOH2337 |
| E | HOH2338 |
| E | HOH2339 |
| E | HOH2341 |
| E | HOH2342 |
| site_id | BC3 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NAP F 263 |
| Chain | Residue |
| F | GLY18 |
| F | ASN20 |
| F | ARG21 |
| F | GLY22 |
| F | ILE23 |
| F | TYR42 |
| F | ARG43 |
| F | SER44 |
| F | ALA45 |
| F | CYS68 |
| F | ASP69 |
| F | VAL70 |
| F | ASN96 |
| F | ALA97 |
| F | GLY98 |
| F | VAL119 |
| F | THR147 |
| F | SER148 |
| F | SER149 |
| F | TYR169 |
| F | LYS173 |
| F | PRO199 |
| F | GLY200 |
| F | VAL202 |
| F | GLN206 |
| F | HOH2059 |
| F | HOH2062 |
| F | HOH2151 |
| F | HOH2236 |
| F | HOH2240 |
| F | HOH2307 |
| F | HOH2308 |
| F | HOH2309 |
| F | HOH2310 |
| F | HOH2312 |
| F | HOH2313 |
| site_id | BC4 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE NAP G 263 |
| Chain | Residue |
| G | GLY18 |
| G | ASN20 |
| G | ARG21 |
| G | GLY22 |
| G | ILE23 |
| G | ARG43 |
| G | SER44 |
| G | ALA45 |
| G | CYS68 |
| G | ASP69 |
| G | VAL70 |
| G | ASN96 |
| G | ALA97 |
| G | GLY98 |
| G | VAL119 |
| G | THR147 |
| G | SER148 |
| G | SER149 |
| G | TYR169 |
| G | LYS173 |
| G | PRO199 |
| G | GLY200 |
| G | VAL202 |
| G | GLN206 |
| G | HOH2030 |
| G | HOH2058 |
| G | HOH2059 |
| G | HOH2067 |
| G | HOH2227 |
| G | HOH2282 |
| G | HOH2283 |
| G | HOH2284 |
| G | HOH2286 |
| G | HOH2287 |
| G | HOH2289 |
| G | HOH2290 |
| G | HOH2291 |
| site_id | BC5 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAP H 263 |
| Chain | Residue |
| H | ASN20 |
| H | ARG21 |
| H | GLY22 |
| H | ILE23 |
| H | TYR42 |
| H | ARG43 |
| H | SER44 |
| H | ALA45 |
| H | CYS68 |
| H | ASP69 |
| H | VAL70 |
| H | ASN96 |
| H | ALA97 |
| H | GLY98 |
| H | VAL119 |
| H | THR147 |
| H | SER148 |
| H | SER149 |
| H | TYR169 |
| H | LYS173 |
| H | PRO199 |
| H | GLY200 |
| H | VAL202 |
| H | GLN206 |
| H | HOH2054 |
| H | HOH2059 |
| H | HOH2232 |
| H | HOH2293 |
| H | HOH2294 |
| H | HOH2295 |
| H | HOH2296 |
| H | HOH2297 |
| H | HOH2298 |
| H | HOH2300 |
| H | HOH2302 |
| site_id | BC6 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAP I 263 |
| Chain | Residue |
| I | ASN20 |
| I | ARG21 |
| I | GLY22 |
| I | ILE23 |
| I | TYR42 |
| I | ARG43 |
| I | SER44 |
| I | ALA45 |
| I | CYS68 |
| I | ASP69 |
| I | VAL70 |
| I | ASN96 |
| I | ALA97 |
| I | GLY98 |
| I | VAL119 |
| I | THR147 |
| I | SER148 |
| I | SER149 |
| I | TYR169 |
| I | LYS173 |
| I | PRO199 |
| I | GLY200 |
| I | VAL202 |
| I | GLN206 |
| I | HOH2062 |
| I | HOH2063 |
| I | HOH2241 |
| I | HOH2302 |
| I | HOH2303 |
| I | HOH2304 |
| I | HOH2305 |
| I | HOH2306 |
| I | HOH2307 |
| I | HOH2308 |
| site_id | BC7 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE NAP J 263 |
| Chain | Residue |
| J | GLY18 |
| J | ASN20 |
| J | ARG21 |
| J | GLY22 |
| J | ILE23 |
| J | TYR42 |
| J | ARG43 |
| J | SER44 |
| J | ALA45 |
| J | CYS68 |
| J | ASP69 |
| J | VAL70 |
| J | ASN96 |
| J | ALA97 |
| J | GLY98 |
| J | VAL119 |
| J | THR147 |
| J | SER148 |
| J | SER149 |
| J | TYR169 |
| J | LYS173 |
| J | PRO199 |
| J | GLY200 |
| J | VAL202 |
| J | GLN206 |
| J | HOH2023 |
| J | HOH2044 |
| J | HOH2163 |
| J | HOH2205 |
| J | HOH2261 |
| J | HOH2262 |
| J | HOH2263 |
| J | HOH2264 |
| J | HOH2265 |
| J | HOH2266 |
| J | HOH2267 |
| J | HOH2268 |
| site_id | BC8 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE NAP K 263 |
| Chain | Residue |
| K | GLY18 |
| K | ASN20 |
| K | ARG21 |
| K | GLY22 |
| K | ILE23 |
| K | TYR42 |
| K | ARG43 |
| K | SER44 |
| K | ALA45 |
| K | CYS68 |
| K | ASP69 |
| K | VAL70 |
| K | ASN96 |
| K | ALA97 |
| K | GLY98 |
| K | VAL119 |
| K | THR147 |
| K | SER148 |
| K | SER149 |
| K | TYR169 |
| K | LYS173 |
| K | PRO199 |
| K | GLY200 |
| K | VAL202 |
| K | THR204 |
| K | GLN206 |
| K | HOH2046 |
| K | HOH2049 |
| K | HOH2136 |
| K | HOH2221 |
| K | HOH2276 |
| K | HOH2277 |
| K | HOH2278 |
| K | HOH2279 |
| K | HOH2281 |
| K | HOH2282 |
| K | HOH2283 |
| K | HOH2284 |
| site_id | BC9 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NAP L 263 |
| Chain | Residue |
| L | ASN20 |
| L | ARG21 |
| L | GLY22 |
| L | ILE23 |
| L | TYR42 |
| L | ARG43 |
| L | SER44 |
| L | ALA45 |
| L | CYS68 |
| L | ASP69 |
| L | VAL70 |
| L | ASN96 |
| L | ALA97 |
| L | GLY98 |
| L | VAL99 |
| L | THR147 |
| L | SER148 |
| L | SER149 |
| L | TYR169 |
| L | LYS173 |
| L | PRO199 |
| L | GLY200 |
| L | VAL202 |
| L | GLN206 |
| L | HOH2060 |
| L | HOH2061 |
| L | HOH2235 |
| L | HOH2239 |
| L | HOH2299 |
| L | HOH2300 |
| L | HOH2301 |
| L | HOH2302 |
| L | HOH2303 |
| L | HOH2304 |
| L | HOH2305 |
| L | HOH2306 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:11335726 |
| Chain | Residue | Details |
| A | MET150 | |
| J | MET150 | |
| K | MET150 | |
| L | MET150 | |
| B | MET150 | |
| C | MET150 | |
| D | MET150 | |
| E | MET150 | |
| F | MET150 | |
| G | MET150 | |
| H | MET150 | |
| I | MET150 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:11335726 |
| Chain | Residue | Details |
| A | ASN170 | |
| J | ASN170 | |
| K | ASN170 | |
| L | ASN170 | |
| B | ASN170 | |
| C | ASN170 | |
| D | ASN170 | |
| E | ASN170 | |
| F | ASN170 | |
| G | ASN170 | |
| H | ASN170 | |
| I | ASN170 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | ACT_SITE: Lowers pKa of active site Tyr => ECO:0000305|PubMed:11335726 |
| Chain | Residue | Details |
| A | ALA174 | |
| J | ALA174 | |
| K | ALA174 | |
| L | ALA174 | |
| B | ALA174 | |
| C | ALA174 | |
| D | ALA174 | |
| E | ALA174 | |
| F | ALA174 | |
| G | ALA174 | |
| H | ALA174 | |
| I | ALA174 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 48 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:L0E2Z4 |
| Chain | Residue | Details |
| A | GLY24 | |
| C | VAL70 | |
| C | ALA130 | |
| C | ASP205 | |
| D | GLY24 | |
| D | VAL70 | |
| D | ALA130 | |
| D | ASP205 | |
| E | GLY24 | |
| E | VAL70 | |
| E | ALA130 | |
| A | VAL70 | |
| E | ASP205 | |
| F | GLY24 | |
| F | VAL70 | |
| F | ALA130 | |
| F | ASP205 | |
| G | GLY24 | |
| G | VAL70 | |
| G | ALA130 | |
| G | ASP205 | |
| H | GLY24 | |
| A | ALA130 | |
| H | VAL70 | |
| H | ALA130 | |
| H | ASP205 | |
| I | GLY24 | |
| I | VAL70 | |
| I | ALA130 | |
| I | ASP205 | |
| J | GLY24 | |
| J | VAL70 | |
| J | ALA130 | |
| A | ASP205 | |
| J | ASP205 | |
| K | GLY24 | |
| K | VAL70 | |
| K | ALA130 | |
| K | ASP205 | |
| L | GLY24 | |
| L | VAL70 | |
| L | ALA130 | |
| L | ASP205 | |
| B | GLY24 | |
| B | VAL70 | |
| B | ALA130 | |
| B | ASP205 | |
| C | GLY24 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 60 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11335726, ECO:0007744|PDB:1H5Q |
| Chain | Residue | Details |
| A | ALA97 | |
| B | THR207 | |
| C | ALA97 | |
| C | ASN170 | |
| C | ALA174 | |
| C | ASN203 | |
| C | THR207 | |
| D | ALA97 | |
| D | ASN170 | |
| D | ALA174 | |
| D | ASN203 | |
| A | ASN170 | |
| D | THR207 | |
| E | ALA97 | |
| E | ASN170 | |
| E | ALA174 | |
| E | ASN203 | |
| E | THR207 | |
| F | ALA97 | |
| F | ASN170 | |
| F | ALA174 | |
| F | ASN203 | |
| A | ALA174 | |
| F | THR207 | |
| G | ALA97 | |
| G | ASN170 | |
| G | ALA174 | |
| G | ASN203 | |
| G | THR207 | |
| H | ALA97 | |
| H | ASN170 | |
| H | ALA174 | |
| H | ASN203 | |
| A | ASN203 | |
| H | THR207 | |
| I | ALA97 | |
| I | ASN170 | |
| I | ALA174 | |
| I | ASN203 | |
| I | THR207 | |
| J | ALA97 | |
| J | ASN170 | |
| J | ALA174 | |
| J | ASN203 | |
| A | THR207 | |
| J | THR207 | |
| K | ALA97 | |
| K | ASN170 | |
| K | ALA174 | |
| K | ASN203 | |
| K | THR207 | |
| L | ALA97 | |
| L | ASN170 | |
| L | ALA174 | |
| L | ASN203 | |
| B | ALA97 | |
| L | THR207 | |
| B | ASN170 | |
| B | ALA174 | |
| B | ASN203 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | SER149 | |
| A | TYR169 | |
| A | LYS173 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| J | SER149 | |
| J | TYR169 | |
| J | LYS173 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| K | SER149 | |
| K | TYR169 | |
| K | LYS173 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| L | SER149 | |
| L | TYR169 | |
| L | LYS173 |
| site_id | CSA13 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | ASN120 | |
| A | TYR169 | |
| A | SER149 | |
| A | LYS173 |
| site_id | CSA14 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | ASN120 | |
| B | TYR169 | |
| B | SER149 | |
| B | LYS173 |
| site_id | CSA15 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | ASN120 | |
| C | TYR169 | |
| C | SER149 | |
| C | LYS173 |
| site_id | CSA16 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | ASN120 | |
| D | TYR169 | |
| D | SER149 | |
| D | LYS173 |
| site_id | CSA17 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | ASN120 | |
| E | TYR169 | |
| E | SER149 | |
| E | LYS173 |
| site_id | CSA18 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | ASN120 | |
| F | TYR169 | |
| F | SER149 | |
| F | LYS173 |
| site_id | CSA19 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| G | ASN120 | |
| G | TYR169 | |
| G | SER149 | |
| G | LYS173 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | SER149 | |
| B | TYR169 | |
| B | LYS173 |
| site_id | CSA20 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| H | ASN120 | |
| H | TYR169 | |
| H | SER149 | |
| H | LYS173 |
| site_id | CSA21 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| I | ASN120 | |
| I | TYR169 | |
| I | SER149 | |
| I | LYS173 |
| site_id | CSA22 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| J | ASN120 | |
| J | TYR169 | |
| J | SER149 | |
| J | LYS173 |
| site_id | CSA23 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| K | ASN120 | |
| K | TYR169 | |
| K | SER149 | |
| K | LYS173 |
| site_id | CSA24 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| L | ASN120 | |
| L | TYR169 | |
| L | SER149 | |
| L | LYS173 |
| site_id | CSA25 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR169 | |
| A | LYS173 |
| site_id | CSA26 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR169 | |
| B | LYS173 |
| site_id | CSA27 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | TYR169 | |
| C | LYS173 |
| site_id | CSA28 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | TYR169 | |
| D | LYS173 |
| site_id | CSA29 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | TYR169 | |
| E | LYS173 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | SER149 | |
| C | TYR169 | |
| C | LYS173 |
| site_id | CSA30 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | TYR169 | |
| F | LYS173 |
| site_id | CSA31 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| G | TYR169 | |
| G | LYS173 |
| site_id | CSA32 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| H | TYR169 | |
| H | LYS173 |
| site_id | CSA33 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| I | TYR169 | |
| I | LYS173 |
| site_id | CSA34 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| J | TYR169 | |
| J | LYS173 |
| site_id | CSA35 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| K | TYR169 | |
| K | LYS173 |
| site_id | CSA36 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| L | TYR169 | |
| L | LYS173 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | SER149 | |
| D | TYR169 | |
| D | LYS173 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | SER149 | |
| E | TYR169 | |
| E | LYS173 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | SER149 | |
| F | TYR169 | |
| F | LYS173 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| G | SER149 | |
| G | TYR169 | |
| G | LYS173 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| H | SER149 | |
| H | TYR169 | |
| H | LYS173 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| I | SER149 | |
| I | TYR169 | |
| I | LYS173 |
