5Z21
The ternary structure of D-lactate dehydrogenase from Fusobacterium nucleatum 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 (NAD+) 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 (NAD+) 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 (NAD+) 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 (NAD+) 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue NAI A 401 |
| Chain | Residue |
| A | TYR102 |
| A | PHE178 |
| A | PRO209 |
| A | THR214 |
| A | THR235 |
| A | GLY236 |
| A | ARG237 |
| A | ASP261 |
| A | HIS298 |
| A | ALA300 |
| A | TYR301 |
| A | ILE107 |
| A | OXM402 |
| A | THR154 |
| A | GLY155 |
| A | LYS156 |
| A | ILE157 |
| A | TYR175 |
| A | ASP176 |
| A | LEU177 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue OXM A 402 |
| Chain | Residue |
| A | CYS79 |
| A | ALA80 |
| A | GLY81 |
| A | TYR102 |
| A | ARG237 |
| A | HIS298 |
| A | TYR301 |
| A | NAI401 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | binding site for residue NAI B 401 |
| Chain | Residue |
| B | TYR102 |
| B | ILE107 |
| B | THR154 |
| B | GLY155 |
| B | LYS156 |
| B | ILE157 |
| B | TYR175 |
| B | ASP176 |
| B | LEU177 |
| B | ASN207 |
| B | PRO209 |
| B | THR214 |
| B | THR235 |
| B | GLY236 |
| B | ARG237 |
| B | ASP261 |
| B | HIS298 |
| B | ALA300 |
| B | TYR301 |
| B | OXM402 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue OXM B 402 |
| Chain | Residue |
| B | CYS79 |
| B | ALA80 |
| B | GLY81 |
| B | TYR102 |
| B | ARG237 |
| B | HIS298 |
| B | TYR301 |
| B | NAI401 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | binding site for residue NAI C 401 |
| Chain | Residue |
| C | TYR102 |
| C | ILE107 |
| C | THR154 |
| C | GLY155 |
| C | LYS156 |
| C | ILE157 |
| C | TYR175 |
| C | ASP176 |
| C | ASN207 |
| C | CYS208 |
| C | PRO209 |
| C | THR214 |
| C | THR235 |
| C | GLY236 |
| C | ARG237 |
| C | ASP261 |
| C | HIS298 |
| C | TYR301 |
| C | OXM402 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue OXM C 402 |
| Chain | Residue |
| C | CYS79 |
| C | ALA80 |
| C | GLY81 |
| C | TYR102 |
| C | ARG237 |
| C | HIS298 |
| C | TYR301 |
| C | NAI401 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | binding site for residue NAI D 401 |
| Chain | Residue |
| D | HIS298 |
| D | ALA300 |
| D | TYR301 |
| D | OXM402 |
| D | HOH522 |
| D | HOH527 |
| D | TYR102 |
| D | ILE107 |
| D | THR154 |
| D | GLY155 |
| D | LYS156 |
| D | ILE157 |
| D | TYR175 |
| D | ASP176 |
| D | LEU177 |
| D | PRO209 |
| D | ASP213 |
| D | THR214 |
| D | THR235 |
| D | GLY236 |
| D | ARG237 |
| D | ASP261 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue OXM D 402 |
| Chain | Residue |
| D | CYS79 |
| D | ALA80 |
| D | GLY81 |
| D | TYR102 |
| D | ARG237 |
| D | HIS298 |
| D | TYR301 |
| D | NAI401 |
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. AGIIGtGKIGqilikilrgfdmk.VIaYD |
| Chain | Residue | Details |
| A | ALA149-ASP176 |
| site_id | PS00670 |
| Number of Residues | 23 |
| Details | D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LYanSDIIsLNcPltkdTkyMiN |
| Chain | Residue | Details |
| A | LEU197-ASN219 |
| site_id | PS00671 |
| Number of Residues | 17 |
| Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKdGvILVNtGRGmLID |
| Chain | Residue | Details |
| A | MET226-ASP242 |
