MolNFT v1 · #68760 · protein
Crystal structure of amino acid-binding act: D-isomer specific 2- hydroxyacid dehydrogenase catalytic domain from brucella melitensis
3K5P · D-3-phosphoglycerate dehydrogenase: “Crystal structure of amino acid-binding act: D-isomer specific 2- hydroxyacid dehydrogenase catalytic domain…”. X-ray diffraction, 1 pocket (best druggability 0.62). MolNFT v1 #68760 on…
- PDB
- 3K5P
- Type
- protein
- Length
- 400 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D-3-phosphoglycerate dehydrogenase
- EC
- 1.1.1.95
- UniProt
- Q2YK82
- Pockets
- 1 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D-3-phosphoglycerate dehydrogenase (EC 1.1.1.95) | protein | 400 | 34% helix, 21% strand | Q2YK82 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 462 | 0.62 | 0.76 | 48 | empty |
Compared structures
- 3K5P · Crystal structure of amino acid-binding ACT: D-isomer specific 2-hydroxyacid… · 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 Q2YK82
- Elsewhere: RCSB PDB 3K5P · PDBe 3K5P · UniProt Q2YK82
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