4B98
The structure of the omega aminotransferase from Pseudomonas aeruginosa
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009102 | biological_process | biotin biosynthetic process |
| A | 0016223 | molecular_function | beta-alanine:pyruvate transaminase activity |
| A | 0019483 | biological_process | beta-alanine biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009102 | biological_process | biotin biosynthetic process |
| B | 0016223 | molecular_function | beta-alanine:pyruvate transaminase activity |
| B | 0019483 | biological_process | beta-alanine biosynthetic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009102 | biological_process | biotin biosynthetic process |
| C | 0016223 | molecular_function | beta-alanine:pyruvate transaminase activity |
| C | 0019483 | biological_process | beta-alanine biosynthetic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009102 | biological_process | biotin biosynthetic process |
| D | 0016223 | molecular_function | beta-alanine:pyruvate transaminase activity |
| D | 0019483 | biological_process | beta-alanine biosynthetic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE PXG A 470 |
| Chain | Residue |
| A | LEU60 |
| A | SER231 |
| A | ASP259 |
| A | VAL261 |
| A | ILE262 |
| A | LYS288 |
| A | ARG414 |
| A | GLN421 |
| A | HOH2180 |
| A | HOH2272 |
| A | HOH2273 |
| A | TRP61 |
| A | HOH2311 |
| A | HOH2408 |
| B | PHE89 |
| B | THR327 |
| A | SER119 |
| A | GLY120 |
| A | SER121 |
| A | TYR153 |
| A | HIS154 |
| A | GLY155 |
| A | GLU226 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PLP A 501 |
| Chain | Residue |
| A | MET196 |
| A | GLY240 |
| A | TYR241 |
| A | LEU242 |
| A | GLN243 |
| A | PHE277 |
| A | GLY278 |
| A | HOH2276 |
| A | HOH2279 |
| A | HOH2306 |
| A | HOH2409 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 502 |
| Chain | Residue |
| A | ASP180 |
| A | HOH2218 |
| A | HOH2219 |
| A | HOH2220 |
| A | HOH2410 |
| D | ASP180 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 503 |
| Chain | Residue |
| A | SER323 |
| A | HOH2331 |
| A | HOH2333 |
| B | MET172 |
| B | PHE173 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE PXG B 470 |
| Chain | Residue |
| A | PHE89 |
| A | THR327 |
| A | HOH2335 |
| A | HOH2336 |
| B | TRP61 |
| B | SER119 |
| B | GLY120 |
| B | SER121 |
| B | TYR153 |
| B | HIS154 |
| B | GLY155 |
| B | GLU226 |
| B | SER231 |
| B | ASP259 |
| B | VAL261 |
| B | ILE262 |
| B | LYS288 |
| B | ARG414 |
| B | GLN421 |
| B | HOH2041 |
| B | HOH2229 |
| B | HOH2269 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PLP B 501 |
| Chain | Residue |
| B | MET196 |
| B | GLY240 |
| B | TYR241 |
| B | LEU242 |
| B | GLN243 |
| B | PHE277 |
| B | GLY278 |
| B | HOH2234 |
| B | HOH2362 |
| B | HOH2365 |
| B | HOH2366 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 502 |
| Chain | Residue |
| B | ASP180 |
| B | HOH2171 |
| B | HOH2172 |
| B | HOH2173 |
| B | HOH2367 |
| C | ASP180 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 503 |
| Chain | Residue |
| A | MET172 |
| A | PHE173 |
| B | SER323 |
| B | HOH2283 |
| B | HOH2285 |
| site_id | AC9 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE PXG C 470 |
| Chain | Residue |
| C | VAL261 |
| C | ILE262 |
| C | LYS288 |
| C | ARG414 |
| C | GLN421 |
| C | HOH2062 |
| C | HOH2177 |
| C | HOH2253 |
| C | HOH2292 |
| C | HOH2387 |
| D | PHE89 |
| D | TYR326 |
| D | THR327 |
| C | TRP61 |
| C | SER119 |
| C | GLY120 |
| C | SER121 |
| C | TYR153 |
| C | HIS154 |
| C | GLY155 |
| C | GLU226 |
| C | SER231 |
| C | ASP259 |
| site_id | BC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP C 501 |
| Chain | Residue |
| C | MET196 |
| C | GLY240 |
| C | TYR241 |
| C | LEU242 |
| C | GLN243 |
| C | PHE277 |
| C | GLY278 |
| C | HOH2255 |
| C | HOH2286 |
| C | HOH2388 |
| C | HOH2389 |
| C | HOH2390 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL C 503 |
| Chain | Residue |
| C | SER323 |
| C | HOH2314 |
| C | HOH2317 |
| D | MET172 |
| D | PHE173 |
| site_id | BC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE PXG D 470 |
| Chain | Residue |
| C | PHE89 |
| C | TYR326 |
| C | THR327 |
| C | HOH2318 |
| C | HOH2319 |
| D | TRP61 |
| D | SER119 |
| D | GLY120 |
| D | SER121 |
| D | TYR153 |
| D | HIS154 |
| D | GLY155 |
| D | GLU226 |
| D | SER231 |
| D | ASP259 |
| D | VAL261 |
| D | ILE262 |
| D | LYS288 |
| D | ARG414 |
| D | GLN421 |
| D | HOH2122 |
| D | HOH2188 |
| D | HOH2228 |
| site_id | BC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PLP D 501 |
| Chain | Residue |
| D | MET196 |
| D | VAL239 |
| D | GLY240 |
| D | TYR241 |
| D | LEU242 |
| D | GLN243 |
| D | PHE277 |
| D | GLY278 |
| D | HOH2191 |
| D | HOH2224 |
| D | HOH2299 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL D 503 |
| Chain | Residue |
| C | MET172 |
| C | PHE173 |
| D | SER323 |
| D | HOH2239 |
| D | HOH2241 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIfDEVit.AFgRlGtysgaeyfgvtp....DLMnvAKqvtNG |
| Chain | Residue | Details |
| A | LEU256-GLY293 |
| site_id | PS00639 |
| Number of Residues | 11 |
| Details | THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. GYHGVNVAGTS |
| Chain | Residue | Details |
| A | GLY152-SER162 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23519665 |
| Chain | Residue | Details |
| A | TRP61 | |
| D | TRP61 | |
| D | ARG414 | |
| D | GLN421 | |
| A | ARG414 | |
| A | GLN421 | |
| B | TRP61 | |
| B | ARG414 | |
| B | GLN421 | |
| C | TRP61 | |
| C | ARG414 | |
| C | GLN421 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY120 | |
| B | GLY120 | |
| C | GLY120 | |
| D | GLY120 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23519665, ECO:0000269|Ref.4 |
| Chain | Residue | Details |
| A | THR327 | |
| B | THR327 | |
| C | THR327 | |
| D | THR327 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
| Chain | Residue | Details |
| A | LYS288 | |
| B | LYS288 | |
| C | LYS288 | |
| D | LYS288 |
