Research workbench
Crystal structure of PHO85-PCL10 complex
Analyse Crystal structure of PHO85-PCL10 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KRD
- Type
- protein
- Length
- 484 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclin-dependent protein kinase PHO85; PHO85 cyclin-10
- EC
- 2.7.11.22
- UniProt
- P17157, P53124
- Pockets
- 7 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclin-dependent protein kinase PHO85 (EC 2.7.11.22) | protein | 294 | 38% helix, 19% strand | P17157 |
| B | PHO85 cyclin-10 | protein | 190 | 60% helix, 3% strand | P53124 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 530 | 0.72 | 0.81 | 55 | empty |
| 2 | 73 | 0.42 | 0.80 | 15 | empty |
| 3 | 102 | 0.40 | 0.77 | 22 | empty |
| 4 | 56 | 0.38 | 0.80 | 12 | empty |
| 5 | 85 | 0.37 | 0.76 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1579 Ų buried · 36 hydrogen bonds · protein-protein
Compared structures
- 4KRD · Crystal Structure of Pho85-Pcl10 Complex · the same entry in another collection · chain A against A, TM-score 1.00
- P53124 · AlphaFold monomer V2.0 prediction for PHO85 cyclin-10 (P53124) · a predicted model of the same protein · chain B against A, TM-score 0.99
- P17157 · AlphaFold monomer V2.0 prediction for cyclin-dependent protein kinase PHO85 (P17157) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P17157
- Every structure of UniProt P53124
- Elsewhere: RCSB PDB 4KRD · PDBe 4KRD · UniProt P17157 · UniProt P53124
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