3ZQA
CRYSTALLOGRAPHIC STRUCTURE OF BETAINE ALDEHYDE DEHYDROGENASE MUTANT C286A FROM PSEUDOMONAS AERUGINOSA IN COMPLEX WITH NADPH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008802 | molecular_function | betaine-aldehyde dehydrogenase 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 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 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 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 | TYR340 |
| A | GLU387 |
| A | NDP1500 |
| A | HOH2402 |
| A | HOH2405 |
| A | HOH2500 |
| A | HOH2551 |
| A | HOH2643 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 1492 |
| Chain | Residue |
| A | TRP444 |
| A | GLY445 |
| A | PG41495 |
| A | HOH2343 |
| A | HOH2603 |
| A | HOH2604 |
| A | HOH2644 |
| A | HOH2645 |
| A | HOH2646 |
| A | MET276 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1493 |
| Chain | Residue |
| A | PHE4 |
| A | GLU5 |
| A | GLN7 |
| A | LYS187 |
| A | GOL1494 |
| A | HOH2013 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1494 |
| Chain | Residue |
| A | GLU5 |
| A | GLU6 |
| A | GLN7 |
| A | LYS8 |
| A | TYR15 |
| A | GOL1493 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PG4 A 1495 |
| Chain | Residue |
| A | GLN157 |
| A | SER447 |
| A | GOL1492 |
| A | EDO1498 |
| A | GOL1499 |
| A | NDP1500 |
| A | HOH2343 |
| A | HOH2346 |
| A | HOH2400 |
| A | HOH2609 |
| A | HOH2646 |
| A | HOH2647 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1496 |
| Chain | Residue |
| A | ARG269 |
| A | GLN422 |
| A | ASN442 |
| B | GLU482 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1497 |
| Chain | Residue |
| A | SER336 |
| A | TYR340 |
| A | GLU386 |
| A | HOH2499 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 1498 |
| Chain | Residue |
| A | ASN153 |
| A | VAL285 |
| A | ALA286 |
| A | THR287 |
| A | PG41495 |
| A | GOL1499 |
| A | NDP1500 |
| A | HOH2445 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1499 |
| Chain | Residue |
| A | TRP161 |
| A | GLU252 |
| A | VAL453 |
| A | GLU464 |
| A | PG41495 |
| A | EDO1498 |
| A | NDP1500 |
| A | HOH2610 |
| site_id | BC1 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE NDP A 1500 |
| Chain | Residue |
| A | HOH2410 |
| A | HOH2496 |
| A | HOH2500 |
| A | HOH2648 |
| A | HOH2649 |
| A | HOH2650 |
| A | ILE149 |
| A | GLY150 |
| A | ALA151 |
| A | TRP152 |
| A | ASN153 |
| A | LYS176 |
| A | SER178 |
| A | GLU179 |
| A | SER208 |
| A | GLY209 |
| A | GLY213 |
| A | PHE227 |
| A | THR228 |
| A | GLY229 |
| A | GLY230 |
| A | THR233 |
| A | VAL237 |
| A | GLU252 |
| A | LEU253 |
| A | GLY254 |
| A | ALA286 |
| A | GLU387 |
| A | PHE389 |
| A | GOL1491 |
| A | PG41495 |
| A | EDO1498 |
| A | GOL1499 |
| A | HOH2341 |
| A | HOH2355 |
| A | HOH2356 |
| A | HOH2377 |
| A | HOH2385 |
| A | HOH2405 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 1501 |
| Chain | Residue |
| A | THR26 |
| A | ILE27 |
| A | ASP93 |
| A | VAL180 |
| A | HOH2091 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K A 1502 |
| Chain | Residue |
| A | LYS457 |
| A | GLY460 |
| A | HOH2344 |
| B | LEU246 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 1491 |
| Chain | Residue |
| A | HOH2636 |
| B | MET276 |
| B | HOH2392 |
| B | HOH2420 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1492 |
| Chain | Residue |
| B | GLN157 |
| B | GOL1495 |
| B | HOH2252 |
| B | HOH2254 |
| B | HOH2326 |
| B | HOH2328 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 1493 |
| Chain | Residue |
| B | PHE4 |
| B | GLU5 |
| B | GLN7 |
| B | LYS187 |
| B | HOH2009 |
| B | HOH2012 |
| B | HOH2017 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1494 |
| Chain | Residue |
| B | GLU6 |
| B | GLN7 |
| B | LYS8 |
| B | TYR15 |
| B | HOH2012 |
| site_id | BC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL B 1495 |
| Chain | Residue |
| B | TRP161 |
| B | GLU252 |
| B | ILE438 |
| B | SER447 |
| B | VAL453 |
| B | GLU464 |
| B | GOL1492 |
| B | NDP1498 |
| B | HOH2254 |
| B | HOH2309 |
| B | HOH2328 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 1496 |
| Chain | Residue |
| B | GLY209 |
| B | ARG210 |
| B | NDP1498 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 1497 |
| Chain | Residue |
| B | SER336 |
| B | GLY339 |
| site_id | CC2 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NDP B 1498 |
| Chain | Residue |
| B | ILE149 |
| B | GLY150 |
| B | ALA151 |
| B | TRP152 |
| B | ASN153 |
| B | LYS176 |
| B | SER178 |
| B | GLU179 |
| B | SER208 |
| B | GLY209 |
| B | PHE227 |
| B | THR228 |
| B | GLY229 |
| B | GLY230 |
| B | THR233 |
| B | VAL237 |
| B | GLU252 |
| B | LEU253 |
| B | GLY254 |
| B | ALA286 |
| B | GLU387 |
| B | PHE389 |
| B | GOL1495 |
| B | GOL1496 |
| B | HOH2261 |
| B | HOH2278 |
| B | HOH2282 |
| B | HOH2294 |
| B | HOH2309 |
| B | HOH2346 |
| B | HOH2364 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 1499 |
| Chain | Residue |
| A | LEU246 |
| A | HOH2392 |
| A | HOH2393 |
| B | LYS457 |
| B | GLY460 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 1500 |
| Chain | Residue |
| B | THR26 |
| B | ILE27 |
| B | ASP93 |
| B | VAL180 |
| B | HOH2066 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 1491 |
| Chain | Residue |
| C | PHE4 |
| C | GLU5 |
| C | GLN7 |
| C | LYS187 |
| site_id | CC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL C 1492 |
| Chain | Residue |
| C | TRP161 |
| C | GLU252 |
| C | GLU464 |
| C | NDP1495 |
| C | TOE1496 |
| C | EDO1497 |
| C | HOH2237 |
| C | HOH2373 |
| C | HOH2405 |
| site_id | CC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 1493 |
| Chain | Residue |
| C | ARG314 |
| C | LEU315 |
| C | THR323 |
| site_id | CC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 1494 |
| Chain | Residue |
| C | SER336 |
| C | GLY339 |
| C | TYR340 |
| site_id | CC9 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NDP C 1495 |
| Chain | Residue |
| C | ILE149 |
| C | GLY150 |
| C | ALA151 |
| C | TRP152 |
| C | ASN153 |
| C | LYS176 |
| C | SER178 |
| C | GLU179 |
| C | GLY207 |
| C | GLY209 |
| C | PHE227 |
| C | THR228 |
| C | GLY229 |
| C | GLY230 |
| C | THR233 |
| C | VAL237 |
| C | GLU252 |
| C | LEU253 |
| C | GLY254 |
| C | ALA286 |
| C | GLU387 |
| C | PHE389 |
| C | GOL1492 |
| C | EDO1497 |
| C | HOH2176 |
| C | HOH2180 |
| C | HOH2213 |
| C | HOH2230 |
| C | HOH2237 |
| C | HOH2296 |
| C | HOH2329 |
| C | HOH2405 |
| C | HOH2408 |
| site_id | DC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TOE C 1496 |
| Chain | Residue |
| C | THR108 |
| C | GLN157 |
| C | SER447 |
| C | GOL1492 |
| C | EDO1497 |
| C | HOH2184 |
| C | HOH2371 |
| C | HOH2405 |
| C | HOH2410 |
| site_id | DC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO C 1497 |
| Chain | Residue |
| C | ASN153 |
| C | VAL285 |
| C | ALA286 |
| C | THR287 |
| C | GOL1492 |
| C | NDP1495 |
| C | TOE1496 |
| C | HOH2263 |
| site_id | DC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K C 1498 |
| Chain | Residue |
| C | THR26 |
| C | ILE27 |
| C | ASP93 |
| C | VAL180 |
| C | HOH2290 |
| site_id | DC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE K C 1499 |
| Chain | Residue |
| C | LYS457 |
| C | GLY460 |
| D | LEU246 |
| site_id | DC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 1491 |
| Chain | Residue |
| D | GLU5 |
| D | GLU6 |
| D | GLN7 |
| D | LYS8 |
| D | TYR15 |
| D | HOH2255 |
| D | HOH2256 |
| site_id | DC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 1492 |
| Chain | Residue |
| D | GLN157 |
| D | GOL1493 |
| D | HOH2243 |
| D | HOH2245 |
| D | HOH2306 |
| D | HOH2406 |
| D | HOH2408 |
| site_id | DC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 1493 |
| Chain | Residue |
| D | TRP161 |
| D | GLU252 |
| D | SER447 |
| D | GLU464 |
| D | GOL1492 |
| D | NDP1496 |
| D | HOH2290 |
| D | HOH2306 |
| D | HOH2406 |
| site_id | DC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 1494 |
| Chain | Residue |
| D | PHE4 |
| D | GLN7 |
| D | LYS187 |
| D | HOH2256 |
| site_id | DC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 1495 |
| Chain | Residue |
| A | ALA2 |
| A | HOH2001 |
| D | LYS236 |
| D | NDP1496 |
| site_id | EC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NDP D 1496 |
| Chain | Residue |
| D | ILE149 |
| D | GLY150 |
| D | ALA151 |
| D | TRP152 |
| D | ASN153 |
| D | LYS176 |
| D | SER178 |
| D | GLU179 |
| D | GLY207 |
| D | SER208 |
| D | GLY209 |
| D | GLY213 |
| D | PHE227 |
| D | THR228 |
| D | GLY229 |
| D | GLY230 |
| D | THR233 |
| D | VAL237 |
| D | GLU252 |
| D | LEU253 |
| D | GLY254 |
| D | ALA286 |
| D | GLU387 |
| D | PHE389 |
| D | GOL1493 |
| D | GOL1495 |
| D | HOH2241 |
| D | HOH2269 |
| D | HOH2278 |
| D | HOH2290 |
| D | HOH2406 |
| D | HOH2407 |
| D | HOH2409 |
| site_id | EC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K D 1497 |
| Chain | Residue |
| D | THR26 |
| D | ILE27 |
| D | ASP93 |
| D | VAL180 |
| D | HOH2079 |
| site_id | EC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K D 1498 |
| Chain | Residue |
| C | LEU246 |
| C | HOH2234 |
| D | LYS457 |
| D | GLY460 |
Functional Information from PROSITE/UniProt
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. MELGGKSP |
| Chain | Residue | Details |
| A | MET251-PRO258 |
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 | GLU252 | |
| B | GLU252 | |
| C | GLU252 | |
| D | GLU252 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:21732915 |
| Chain | Residue | Details |
| A | ALA286 | |
| B | ALA286 | |
| C | ALA286 | |
| D | ALA286 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 28 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LEU246 | |
| A | LYS457 | |
| A | GLY460 | |
| B | THR26 | |
| B | ILE27 | |
| B | ASP93 | |
| B | VAL180 | |
| B | LEU246 | |
| B | LYS457 | |
| B | GLY460 | |
| C | THR26 | |
| C | ILE27 | |
| C | ASP93 | |
| C | VAL180 | |
| C | LEU246 | |
| C | LYS457 | |
| C | GLY460 | |
| D | THR26 | |
| D | ILE27 | |
| D | ASP93 | |
| D | VAL180 | |
| D | LEU246 | |
| D | LYS457 | |
| D | GLY460 | |
| A | THR26 | |
| A | ILE27 | |
| A | ASP93 | |
| A | VAL180 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21732915, ECO:0007744|PDB:2WOX |
| Chain | Residue | Details |
| B | GLY230 | |
| B | GLU387 | |
| C | GLY150 | |
| C | LYS176 | |
| C | GLY209 | |
| C | GLY230 | |
| C | GLU387 | |
| D | GLY150 | |
| D | LYS176 | |
| D | GLY209 | |
| D | GLY230 | |
| D | GLU387 | |
| A | GLY150 | |
| A | LYS176 | |
| A | GLY209 | |
| A | GLY230 | |
| A | GLU387 | |
| B | GLY150 | |
| B | LYS176 | |
| B | GLY209 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: covalent => ECO:0000269|PubMed:21732915, ECO:0007744|PDB:2WOX |
| Chain | Residue | Details |
| A | ALA286 | |
| B | ALA286 | |
| C | ALA286 | |
| D | ALA286 |
| 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 | ALA286 | |
| B | ALA286 | |
| C | ALA286 | |
| D | ALA286 |
