Research workbench
Last common ancestor of hmppk and PLK/HMPPK vitamin kinases
Analyse Last common ancestor of hmppk and PLK/HMPPK vitamin kinases in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7L07
- Type
- protein
- Length
- 214 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ancestral protein ancc
- EC
- 2.7.1.49
- Ligands
- AF3
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ancestral protein ancc (EC 2.7.1.49) | protein | 214 | 47% helix, 20% strand | — |
Ligands and binding sites
- AF3 · Aluminum fluoride · ligand · 3 copies · 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 | 99 | 0.52 | 0.82 | 19 | empty |
| 2 | 66 | 0.33 | 0.76 | 17 | empty |
Compared structures
- 7L07 · Last common ancestor of HMPPK and PLK/HMPPK vitamin kinases · 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
- Elsewhere: RCSB PDB 7L07 · PDBe 7L07
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