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Crystal structure of pkciota in complex with inhibitor
Analyse Crystal structure of pkciota in complex with inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ILZ
- Type
- protein
- Length
- 1,268 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein kinase C iota type
- EC
- 2.7.11.13
- UniProt
- P41743
- Ligands
- AFU
- Pockets
- 19 · best druggability 0.77
Structure
x-ray diffraction · 4 distinct chains · 32% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein kinase C iota type (EC 2.7.11.13) | protein | 320 | 31% helix, 15% strand | P41743 |
| C | Protein kinase C iota type (EC 2.7.11.13) | protein | 317 | 32% helix, 15% strand | P41743 |
| E | Protein kinase C iota type (EC 2.7.11.13) | protein | 316 | 33% helix, 13% strand | P41743 |
| G | Protein kinase C iota type (EC 2.7.11.13) | protein | 315 | 34% helix, 13% strand | P41743 |
Ligands and binding sites
- AFU · 2-amino-5-[3-(piperazin-1-yl)phenyl]-N-(pyridin-4-yl) pyridine-3-carboxamide · ligand · 4 copies · chains A, C, E, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1111 | 0.77 | 0.79 | 115 | AFU |
| 2 | 624 | 0.73 | 0.80 | 68 | AFU |
| 3 | 416 | 0.73 | 0.83 | 38 | AFU |
| 4 | 488 | 0.70 | 0.80 | 54 | AFU |
| 5 | 665 | 0.67 | 0.76 | 64 | empty |
Interfaces
3 interfaces between chains.
- A–G · 305 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 283 Ų buried · 1 hydrogen bond · protein-protein
- A–E · 199 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (phosphorylation).
Compared structures
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 P41743
- Elsewhere: RCSB PDB 6ILZ · PDBe 6ILZ · UniProt P41743
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