Research workbench
Human ikb kinase beta
Analyse Human ikb kinase beta in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KIK
- Type
- protein
- Length
- 1,269 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- EC
- 2.7.11.10
- UniProt
- O14920
- Ligands
- KSA
- Pockets
- 12 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inhibitor of nuclear factor kappa-B kinase subunit beta (EC 2.7.11.10) | protein | 619 | 54% helix, 13% strand | O14920 |
| B | Inhibitor of nuclear factor kappa-B kinase subunit beta (EC 2.7.11.10) | protein | 650 | 52% helix, 14% strand | O14920 |
Ligands and binding sites
- KSA · K-252A · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 548 | 0.73 | 0.81 | 45 | empty |
| 2 | 448 | 0.71 | 0.81 | 53 | empty |
| 3 | 518 | 0.70 | 0.80 | 45 | empty |
| 4 | 481 | 0.67 | 0.78 | 44 | KSA |
| 5 | 406 | 0.64 | 0.78 | 41 | KSA |
Interfaces
1 interface between chains.
- A–B · 1634 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 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 O14920
- Elsewhere: RCSB PDB 4KIK · PDBe 4KIK · UniProt O14920
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