Research workbench
Kdpgal complexed to kdpgal
Analyse Kdpgal complexed to kdpgal in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2V82
- Type
- protein
- Length
- 205 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2-dehydro-3-deoxy-6-phosphogalactonate aldolase
- EC
- 4.1.2.21
- UniProt
- Q6BF16
- Ligands
- KDP
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2-dehydro-3-deoxy-6-phosphogalactonate aldolase (EC 4.1.2.21) | protein | 205 | 45% helix, 17% strand | Q6BF16 |
Ligands and binding sites
- KDP · 2-keto-deoxy-galactose · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.34 | 0.77 | 15 | KDP |
Modifications
Observed in the structure: 2 modified, 1 covalent (engineered, covalent ligand).
Compared structures
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 Q6BF16
- Elsewhere: RCSB PDB 2V82 · PDBe 2V82 · UniProt Q6BF16
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