2XDR
CRYSTALLOGRAPHIC STRUCTURE OF BETAINE ALDEHYDE DEHYDROGENASE MUTANT E252A FROM PSEUDOMONAS AERUGINOSA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008802 | molecular_function | betaine-aldehyde dehydrogenase (NAD+) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| A | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008802 | molecular_function | betaine-aldehyde dehydrogenase (NAD+) activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0008802 | molecular_function | betaine-aldehyde dehydrogenase (NAD+) activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| C | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0008802 | molecular_function | betaine-aldehyde dehydrogenase (NAD+) activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| D | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1491 |
| Chain | Residue |
| A | ILE438 |
| A | SER447 |
| A | VAL453 |
| A | GLU464 |
| A | TOE1492 |
| A | HOH2530 |
| A | HOH2531 |
| A | HOH2534 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TOE A 1492 |
| Chain | Residue |
| A | ILE158 |
| A | SER447 |
| A | GOL1491 |
| A | HOH2086 |
| A | HOH2259 |
| A | HOH2309 |
| A | HOH2342 |
| A | HOH2532 |
| A | HOH2533 |
| A | HOH2534 |
| A | GLN157 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K A 1493 |
| Chain | Residue |
| A | THR26 |
| A | ILE27 |
| A | ASP93 |
| A | VAL180 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE K A 1494 |
| Chain | Residue |
| A | LYS457 |
| A | GLY460 |
| B | LEU246 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NDP A 5502 |
| Chain | Residue |
| A | ILE149 |
| A | GLY150 |
| A | LYS176 |
| A | SER178 |
| A | GLU179 |
| A | SER208 |
| A | GLY209 |
| A | GLY213 |
| A | GLN214 |
| A | PHE227 |
| A | GLY230 |
| A | THR233 |
| A | VAL237 |
| A | HOH2296 |
| A | HOH2536 |
| A | HOH2537 |
| A | HOH2538 |
| A | HOH2540 |
| A | HOH2541 |
| A | HOH2542 |
| A | HOH2543 |
| A | HOH2544 |
| A | HOH2545 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 1491 |
| Chain | Residue |
| B | CYS286 |
| B | ILE438 |
| B | SER447 |
| B | VAL453 |
| B | GLU464 |
| B | GOL1492 |
| B | HOH2351 |
| B | HOH2355 |
| B | HOH2381 |
| B | HOH2383 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1492 |
| Chain | Residue |
| B | TYR154 |
| B | GLN157 |
| B | GOL1491 |
| B | HOH2382 |
| B | HOH2383 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1493 |
| Chain | Residue |
| B | PHE4 |
| B | GLN7 |
| B | LYS187 |
| B | HOH2007 |
| B | HOH2014 |
| B | HOH2384 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1494 |
| Chain | Residue |
| B | GLU5 |
| B | GLU6 |
| B | GLN7 |
| B | LYS8 |
| B | TYR15 |
| B | HOH2384 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE K B 5500 |
| Chain | Residue |
| A | LEU246 |
| B | LYS457 |
| B | GLY460 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K B 5501 |
| Chain | Residue |
| B | THR26 |
| B | ILE27 |
| B | ASP93 |
| B | VAL180 |
| site_id | BC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NDP B 5502 |
| Chain | Residue |
| B | HOH2387 |
| B | HOH2388 |
| B | HOH2390 |
| B | ILE149 |
| B | GLY150 |
| B | LYS176 |
| B | SER178 |
| B | GLU179 |
| B | GLY207 |
| B | GLY209 |
| B | GLY213 |
| B | GLN214 |
| B | PHE227 |
| B | GLY229 |
| B | GLY230 |
| B | THR233 |
| B | VAL237 |
| B | HOH2385 |
| B | HOH2386 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 1491 |
| Chain | Residue |
| C | PHE4 |
| C | GLN7 |
| C | LYS187 |
| C | HOH2325 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 1492 |
| Chain | Residue |
| C | GLN157 |
| C | VAL285 |
| C | GOL1493 |
| C | HOH2143 |
| C | HOH2146 |
| C | HOH2326 |
| C | HOH2327 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 1493 |
| Chain | Residue |
| C | CYS286 |
| C | GLU464 |
| C | GOL1492 |
| C | HOH2174 |
| C | HOH2294 |
| C | HOH2328 |
| C | HOH2329 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 1494 |
| Chain | Residue |
| C | ARG314 |
| C | LEU315 |
| C | ASP320 |
| C | THR323 |
| C | HOH2330 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 1495 |
| Chain | Residue |
| C | SER336 |
| C | GLY339 |
| C | TYR340 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K C 1496 |
| Chain | Residue |
| C | THR26 |
| C | ILE27 |
| C | ASP93 |
| C | VAL180 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE K C 1497 |
| Chain | Residue |
| C | LYS457 |
| C | GLY460 |
| D | LEU246 |
| site_id | CC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NDP C 5502 |
| Chain | Residue |
| C | ILE149 |
| C | GLY150 |
| C | LYS176 |
| C | SER178 |
| C | GLU179 |
| C | GLY207 |
| C | GLY209 |
| C | GLY213 |
| C | GLN214 |
| C | PHE227 |
| C | GLY229 |
| C | GLY230 |
| C | THR233 |
| C | VAL237 |
| C | HOH2332 |
| C | HOH2333 |
| C | HOH2334 |
| C | HOH2335 |
| C | HOH2336 |
| C | HOH2337 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 1491 |
| Chain | Residue |
| D | GLU5 |
| D | GLU6 |
| D | GLN7 |
| D | LYS8 |
| D | TYR15 |
| D | HOH2399 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 1492 |
| Chain | Residue |
| D | GLN157 |
| D | VAL285 |
| D | GOL1493 |
| D | HOH2283 |
| D | HOH2395 |
| D | HOH2396 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 1493 |
| Chain | Residue |
| D | CYS286 |
| D | SER447 |
| D | GLU464 |
| D | GOL1492 |
| D | HOH2397 |
| site_id | CC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 1494 |
| Chain | Residue |
| D | PHE4 |
| D | GLU5 |
| D | GLN7 |
| D | LYS187 |
| D | HOH2398 |
| D | HOH2399 |
| site_id | CC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K D 1495 |
| Chain | Residue |
| D | THR26 |
| D | ILE27 |
| D | ASP93 |
| D | VAL180 |
| site_id | CC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE K D 1496 |
| Chain | Residue |
| C | LEU246 |
| D | LYS457 |
| D | GLY460 |
| site_id | CC9 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NDP D 5502 |
| Chain | Residue |
| D | ILE149 |
| D | GLY150 |
| D | LYS176 |
| D | SER178 |
| D | GLU179 |
| D | GLY207 |
| D | SER208 |
| D | GLY209 |
| D | GLY213 |
| D | GLN214 |
| D | PHE227 |
| D | THR228 |
| D | GLY229 |
| D | GLY230 |
| D | THR233 |
| D | VAL237 |
| D | HOH2223 |
| D | HOH2400 |
| D | HOH2401 |
| D | HOH2404 |
| D | HOH2406 |
| D | HOH2407 |
| D | HOH2408 |
| D | HOH2410 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfSSGQVCTNGT |
| Chain | Residue | Details |
| A | PHE279-THR290 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Charge relay system => ECO:0000255|HAMAP-Rule:MF_00804, ECO:0000269|PubMed:19013472 |
| Chain | Residue | Details |
| A | LYS162 | |
| A | GLU464 | |
| B | LYS162 | |
| B | GLU464 | |
| C | LYS162 | |
| C | GLU464 | |
| D | LYS162 | |
| D | GLU464 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00804, ECO:0000269|PubMed:19013472 |
| Chain | Residue | Details |
| A | ALA252 | |
| B | ALA252 | |
| C | ALA252 | |
| D | ALA252 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:21732915 |
| Chain | Residue | Details |
| A | CYS286 | |
| B | CYS286 | |
| C | CYS286 | |
| D | CYS286 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 28 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | THR26 | |
| B | ASP93 | |
| B | VAL180 | |
| B | LEU246 | |
| B | LYS457 | |
| B | GLY460 | |
| C | THR26 | |
| C | ILE27 | |
| C | ASP93 | |
| C | VAL180 | |
| C | LEU246 | |
| A | ILE27 | |
| C | LYS457 | |
| C | GLY460 | |
| D | THR26 | |
| D | ILE27 | |
| D | ASP93 | |
| D | VAL180 | |
| D | LEU246 | |
| D | LYS457 | |
| D | GLY460 | |
| A | ASP93 | |
| A | VAL180 | |
| A | LEU246 | |
| A | LYS457 | |
| A | GLY460 | |
| B | THR26 | |
| B | ILE27 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21732915, ECO:0007744|PDB:2WOX |
| Chain | Residue | Details |
| A | GLY150 | |
| B | GLU387 | |
| C | GLY150 | |
| C | LYS176 | |
| C | GLY209 | |
| C | GLY230 | |
| C | GLU387 | |
| D | GLY150 | |
| D | LYS176 | |
| D | GLY209 | |
| D | GLY230 | |
| A | LYS176 | |
| D | GLU387 | |
| A | GLY209 | |
| A | GLY230 | |
| A | GLU387 | |
| B | GLY150 | |
| B | LYS176 | |
| B | GLY209 | |
| B | GLY230 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: covalent => ECO:0000269|PubMed:21732915, ECO:0007744|PDB:2WOX |
| Chain | Residue | Details |
| A | CYS286 | |
| B | CYS286 | |
| C | CYS286 | |
| D | CYS286 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | SITE: Seems to be a necessary countercharge to the potassium cations |
| Chain | Residue | Details |
| A | GLU248 | |
| B | GLU248 | |
| C | GLU248 | |
| D | GLU248 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000255|HAMAP-Rule:MF_00804, ECO:0000269|PubMed:19013472 |
| Chain | Residue | Details |
| A | CYS286 | |
| B | CYS286 | |
| C | CYS286 | |
| D | CYS286 |
