MolNFT v2 · #151539 · protein
Crystal structure of human Plk1-PBD in complex with WSSSLATPPTLSSpTVLI phosphopeptide from BRCA2
6GY2: “Crystal structure of human Plk1-PBD in complex with WSSSLATPPTLSSpTVLI phosphopeptide from BRCA2”. X-ray diffraction at 3.11. MolNFT v2 #151539 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6GY2
- Type
- protein
- Length
- 472 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.11
- Source
- Homo sapiens; SYNTHETIC CONSTRUCT
- UniProt
- P53350
Structure
x-ray diffraction · resolution 3.11 · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 224 | — | P53350 |
| B | — | protein | 224 | — | P53350 |
| C, D | — | protein | 12 | — | — |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6GY2 · Crystal structure of human PLK1-pbd in complex with wssslatpptlssptvli phosphopeptide… · the same entry in another collection · chain A against A, TM-score 1.00
- P53350 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase PLK1 (P53350) · a predicted model of the same protein · chain B against A, TM-score 0.94
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 P53350
- Elsewhere: RCSB PDB 6GY2 · PDBe 6GY2 · UniProt P53350
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.