Research workbench
Crystal structure of PKM2-K422R mutant bound with fbp
Analyse Crystal structure of PKM2-K422R mutant bound with fbp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RPP
- Type
- protein
- Length
- 1,623 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pyruvate kinase pkm
- EC
- 2.7.1.40
- UniProt
- P14618
- Ligands
- FBP
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 4 distinct chains · 48% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pyruvate kinase pkm (EC 2.7.1.40) | protein | 411 | 48% helix, 16% strand | P14618 |
| B | Pyruvate kinase pkm (EC 2.7.1.40) | protein | 408 | 47% helix, 16% strand | P14618 |
| C | Pyruvate kinase pkm (EC 2.7.1.40) | protein | 396 | 49% helix, 16% strand | P14618 |
| D | Pyruvate kinase pkm (EC 2.7.1.40) | protein | 408 | 49% helix, 16% strand | P14618 |
Ligands and binding sites
- FBP · 1,6-di-O-phosphono-beta-D-fructofuranose · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 390 | 0.87 | 0.95 | 51 | empty |
| 2 | 389 | 0.86 | 0.94 | 43 | empty |
| 3 | 704 | 0.74 | 0.80 | 54 | empty |
| 4 | 58 | 0.59 | 0.91 | 21 | empty |
| 5 | 127 | 0.59 | 0.85 | 29 | FBP |
Interfaces
5 interfaces between chains.
- A–B · 2516 Ų buried · 41 hydrogen bonds · protein-protein
- C–D · 2454 Ų buried · 35 hydrogen bonds · protein-protein
- B–D · 1168 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 1136 Ų buried · 20 hydrogen bonds · protein-protein
- A–D · 14 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4RPP · crystal structure of PKM2-K422R mutant bound with FBP · 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 P14618
- Elsewhere: RCSB PDB 4RPP · PDBe 4RPP · UniProt P14618
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