Research workbench
Structure of wild type GLYOXYLATE/HYDROXYPYRUVATE reductase a from escherichia COLI in complex with phosphate and NADP+
Analyse Structure of wild type GLYOXYLATE/HYDROXYPYRUVATE reductase a from escherichia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JQH
- Type
- protein
- Length
- 313 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GLYOXYLATE/HYDROXYPYRUVATE reductase a
- EC
- 1.1.1.79, 1.1.1.81
- UniProt
- A0A140NAE3
- Ligands
- NAP, PO4
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GLYOXYLATE/HYDROXYPYRUVATE reductase a (EC 1.1.1.79, 1.1.1.81) | protein | 313 | 34% helix, 18% strand | A0A140NAE3 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- PO4 · Phosphate ion · ion · 3 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 500 | 0.73 | 0.82 | 59 | NAP, PO4 |
| 2 | 55 | 0.28 | 0.75 | 14 | empty |
Compared structures
- 7JQH · Structure of wild type Glyoxylate/Hydroxypyruvate reductase A from Escherichia Coli in… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A0A140NAE3
- Elsewhere: RCSB PDB 7JQH · PDBe 7JQH · UniProt A0A140NAE3
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