3WNV
Crystal structure of a glyoxylate reductase from Paecilomyes thermophila
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| 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 | 0016618 | molecular_function | hydroxypyruvate reductase [NAD(P)H] activity |
| A | 0030267 | molecular_function | glyoxylate reductase (NADPH) activity |
| A | 0051287 | molecular_function | NAD binding |
| B | 0005829 | cellular_component | cytosol |
| 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 | 0016618 | molecular_function | hydroxypyruvate reductase [NAD(P)H] activity |
| B | 0030267 | molecular_function | glyoxylate reductase (NADPH) activity |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 401 |
| Chain | Residue |
| A | ASN58 |
| A | ALA87 |
| A | GLY88 |
| A | ARG244 |
| A | HOH521 |
| A | HOH582 |
| A | HOH603 |
| A | HOH622 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 401 |
| Chain | Residue |
| B | ALA87 |
| B | GLY88 |
| B | ARG244 |
| B | HOH515 |
| B | HOH539 |
| B | HOH551 |
| B | HOH650 |
| B | ASN58 |
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. LGILGmGGIGrevarrarafgmn.IIyHN |
| Chain | Residue | Details |
| A | LEU157-ASN184 |
| site_id | PS00671 |
| Number of Residues | 17 |
| Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKdGvVIVNtARGaLID |
| Chain | Residue | Details |
| A | MET233-ASP249 |






