5Z20
The ternary structure of D-lactate dehydrogenase from Pseudomonas aeruginosa with NADH and oxamate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008720 | molecular_function | D-lactate dehydrogenase activity |
| 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 | 0051287 | molecular_function | NAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0008720 | molecular_function | D-lactate dehydrogenase activity |
| 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 | 0051287 | molecular_function | NAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0008720 | molecular_function | D-lactate dehydrogenase activity |
| 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 | 0051287 | molecular_function | NAD binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0008720 | molecular_function | D-lactate dehydrogenase activity |
| 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 | 0051287 | molecular_function | NAD binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0008720 | molecular_function | D-lactate dehydrogenase activity |
| 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 | 0051287 | molecular_function | NAD binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0008720 | molecular_function | D-lactate dehydrogenase activity |
| 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 | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue FMT A 401 |
| Chain | Residue |
| A | ARG128 |
| B | HOH567 |
| C | ARG128 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | binding site for residue NAI A 402 |
| Chain | Residue |
| A | PRO175 |
| A | PRO179 |
| A | HIS204 |
| A | CYS205 |
| A | PRO206 |
| A | THR211 |
| A | THR232 |
| A | GLY233 |
| A | ARG234 |
| A | ASP258 |
| A | HIS295 |
| A | ALA297 |
| A | PHE298 |
| A | OXM403 |
| A | HOH514 |
| A | HOH546 |
| A | HOH570 |
| A | HOH579 |
| A | HOH580 |
| A | HOH586 |
| A | HOH592 |
| A | HOH595 |
| A | HOH609 |
| A | HOH626 |
| A | HOH664 |
| A | HOH668 |
| A | TYR100 |
| A | VAL105 |
| A | GLY153 |
| A | GLN154 |
| A | ILE155 |
| A | ASP174 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue OXM A 403 |
| Chain | Residue |
| A | VAL52 |
| A | SER76 |
| A | ALA77 |
| A | GLY78 |
| A | TYR100 |
| A | ARG234 |
| A | HIS295 |
| A | PHE298 |
| A | NAI402 |
| A | HOH657 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue PGE A 404 |
| Chain | Residue |
| A | ASN80 |
| A | HIS81 |
| A | VAL82 |
| A | ASP83 |
| A | HOH556 |
| A | HOH684 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue PEG A 405 |
| Chain | Residue |
| A | PHE140 |
| A | LYS145 |
| A | ASP199 |
| A | LYS224 |
| A | GLY226 |
| A | HOH536 |
| site_id | AC6 |
| Number of Residues | 28 |
| Details | binding site for residue NAI B 401 |
| Chain | Residue |
| B | TYR100 |
| B | THR152 |
| B | GLY153 |
| B | GLN154 |
| B | ILE155 |
| B | ASP174 |
| B | PRO175 |
| B | HIS204 |
| B | CYS205 |
| B | PRO206 |
| B | THR211 |
| B | THR232 |
| B | GLY233 |
| B | ARG234 |
| B | ASP258 |
| B | HIS295 |
| B | ALA297 |
| B | PHE298 |
| B | OXM402 |
| B | HOH516 |
| B | HOH540 |
| B | HOH546 |
| B | HOH549 |
| B | HOH557 |
| B | HOH562 |
| B | HOH570 |
| B | HOH606 |
| B | HOH618 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue OXM B 402 |
| Chain | Residue |
| B | VAL52 |
| B | SER76 |
| B | ALA77 |
| B | GLY78 |
| B | TYR100 |
| B | ARG234 |
| B | HIS295 |
| B | PHE298 |
| B | NAI401 |
| site_id | AC8 |
| Number of Residues | 30 |
| Details | binding site for residue NAI C 401 |
| Chain | Residue |
| C | ASP174 |
| C | PRO175 |
| C | HIS204 |
| C | CYS205 |
| C | PRO206 |
| C | THR211 |
| C | THR232 |
| C | GLY233 |
| C | ARG234 |
| C | ASP258 |
| C | HIS295 |
| C | ALA297 |
| C | PHE298 |
| C | OXM402 |
| C | HOH507 |
| C | HOH525 |
| C | HOH531 |
| C | HOH544 |
| C | HOH553 |
| C | HOH558 |
| C | HOH565 |
| C | HOH579 |
| C | HOH609 |
| C | HOH613 |
| C | HOH629 |
| C | TYR100 |
| C | GLY153 |
| C | GLN154 |
| C | ILE155 |
| C | TYR173 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | binding site for residue OXM C 402 |
| Chain | Residue |
| C | VAL52 |
| C | SER76 |
| C | ALA77 |
| C | GLY78 |
| C | TYR100 |
| C | ARG234 |
| C | HIS295 |
| C | PHE298 |
| C | NAI401 |
| C | HOH643 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue PGE C 403 |
| Chain | Residue |
| C | ASN80 |
| C | VAL82 |
| C | ASP83 |
| C | HOH515 |
| C | HOH536 |
| C | HOH637 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue FMT D 401 |
| Chain | Residue |
| A | HOH612 |
| B | ARG128 |
| D | ARG128 |
| site_id | AD3 |
| Number of Residues | 30 |
| Details | binding site for residue NAI D 402 |
| Chain | Residue |
| D | TYR100 |
| D | GLY153 |
| D | GLN154 |
| D | ILE155 |
| D | TYR173 |
| D | ASP174 |
| D | PRO175 |
| D | HIS204 |
| D | CYS205 |
| D | PRO206 |
| D | THR211 |
| D | THR232 |
| D | GLY233 |
| D | ARG234 |
| D | ASP258 |
| D | HIS295 |
| D | ALA297 |
| D | PHE298 |
| D | OXM403 |
| D | HOH525 |
| D | HOH527 |
| D | HOH543 |
| D | HOH544 |
| D | HOH560 |
| D | HOH577 |
| D | HOH581 |
| D | HOH591 |
| D | HOH600 |
| D | HOH630 |
| D | HOH641 |
| site_id | AD4 |
| Number of Residues | 9 |
| Details | binding site for residue OXM D 403 |
| Chain | Residue |
| D | VAL52 |
| D | SER76 |
| D | ALA77 |
| D | GLY78 |
| D | TYR100 |
| D | ARG234 |
| D | HIS295 |
| D | NAI402 |
| D | HOH642 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue PGE D 404 |
| Chain | Residue |
| D | ASN80 |
| D | VAL82 |
| D | ASP83 |
| D | HOH508 |
| site_id | AD6 |
| Number of Residues | 27 |
| Details | binding site for residue NAI E 401 |
| Chain | Residue |
| E | TYR100 |
| E | GLY153 |
| E | GLN154 |
| E | ILE155 |
| E | TYR173 |
| E | ASP174 |
| E | PRO175 |
| E | HIS204 |
| E | CYS205 |
| E | PRO206 |
| E | THR211 |
| E | THR232 |
| E | GLY233 |
| E | ARG234 |
| E | ASP258 |
| E | HIS295 |
| E | ALA297 |
| E | PHE298 |
| E | OXM402 |
| E | HOH517 |
| E | HOH521 |
| E | HOH535 |
| E | HOH547 |
| E | HOH557 |
| E | HOH560 |
| E | HOH597 |
| E | HOH615 |
| site_id | AD7 |
| Number of Residues | 9 |
| Details | binding site for residue OXM E 402 |
| Chain | Residue |
| E | VAL52 |
| E | SER76 |
| E | ALA77 |
| E | GLY78 |
| E | TYR100 |
| E | ARG234 |
| E | HIS295 |
| E | PHE298 |
| E | NAI401 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue PG4 E 403 |
| Chain | Residue |
| E | ASN80 |
| E | HIS81 |
| E | VAL82 |
| E | ASP83 |
| E | HOH506 |
| site_id | AD9 |
| Number of Residues | 27 |
| Details | binding site for residue NAI F 401 |
| Chain | Residue |
| F | TYR100 |
| F | VAL105 |
| F | GLY153 |
| F | GLN154 |
| F | ILE155 |
| F | TYR173 |
| F | ASP174 |
| F | PRO175 |
| F | HIS204 |
| F | CYS205 |
| F | PRO206 |
| F | THR211 |
| F | THR232 |
| F | GLY233 |
| F | ARG234 |
| F | ASP258 |
| F | HIS295 |
| F | ALA297 |
| F | PHE298 |
| F | OXM402 |
| F | HOH502 |
| F | HOH532 |
| F | HOH547 |
| F | HOH551 |
| F | HOH569 |
| F | HOH572 |
| F | HOH578 |
| site_id | AE1 |
| Number of Residues | 9 |
| Details | binding site for residue OXM F 402 |
| Chain | Residue |
| F | SER76 |
| F | ALA77 |
| F | GLY78 |
| F | TYR100 |
| F | ARG234 |
| F | HIS295 |
| F | PHE298 |
| F | NAI401 |
| F | HOH588 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue PGE F 403 |
| Chain | Residue |
| F | ASN80 |
| F | VAL82 |
| F | ASP83 |
| F | HOH501 |
Functional Information from PROSITE/UniProt
| site_id | PS00065 |
| Number of Residues | 28 |
| Details | D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. VGVIGtGQIGetfarimagfgce.LLaYD |
| Chain | Residue | Details |
| A | VAL147-ASP174 |
| site_id | PS00670 |
| Number of Residues | 23 |
| Details | D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LLaeSDIVsLHcPltadTrhLiD |
| Chain | Residue | Details |
| A | LEU194-ASP216 |
| site_id | PS00671 |
| Number of Residues | 17 |
| Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKpGaMLINtGRGaLVN |
| Chain | Residue | Details |
| A | MET223-ASN239 |
