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 |