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 activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
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 | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
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 | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
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 | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
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 |