Research workbench
Crystal structure of human PKM2 in complex with L-aspartate
Analyse Crystal structure of human PKM2 in complex with L-aspartate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V75
- Type
- protein
- Length
- 1,970 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P14618
- Ligands
- FBP, OXL, K, MG, CL
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | — | protein | 518 | — | P14618 |
| A | — | protein | 509 | — | P14618 |
| B | — | protein | 513 | — | P14618 |
| D | — | protein | 430 | — | P14618 |
Ligands and binding sites
- FBP · 1,6-di-O-phosphono-beta-D-fructofuranose · ligand · 4 copies · chains C, A, B, D
- OXL · Oxalate ion · ligand · chains C
- K · Potassium ion · metal · 6 copies · chains C, A, B, D
- MG · Magnesium ion · metal · 4 copies · chains C, A, B, D
- CL · Chloride ion · ion · chains C
- GOL · Glycerol · additive · 12 copies · chains C, A, B, D
- PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6V75 · Crystal Structure of Human PKM2 in Complex with L-aspartate · the same entry in another collection · chain D against D, 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 6V75 · PDBe 6V75 · UniProt P14618
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.