MolNFT v1 · #85854 · protein
Crystal structure of the human KLHL11-CUL3 complex at 2.8A resolution
4AP2 · Kelch-like protein 11: “Crystal structure of the human KLHL11-CUL3 complex at 2.8A resolution”. X-ray diffraction, 2 ligands (IOD, CL), 3 pockets (best druggability 0.53). MolNFT v1 #85854 on GenesisL1: 3D structure, binding sites…
- PDB
- 4AP2
- Type
- protein
- Length
- 625 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kelch-like protein 11; Cullin-3
- UniProt
- Q9NVR0, Q13618
- Ligands
- IOD, CL
- Pockets
- 3 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 71% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kelch-like protein 11 | protein | 266 | 61% helix, 4% strand | Q9NVR0 |
| B | Cullin-3 | protein | 359 | 79% helix, 0% strand | Q13618 |
Ligands and binding sites
- IOD · Iodide ion · ion · chains A
- CL · Chloride ion · ion · chains B
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 145 | 0.53 | 0.81 | 25 | empty |
| 2 | 96 | 0.37 | 0.75 | 23 | empty |
| 3 | 62 | 0.31 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1564 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 4AP2 · Crystal structure of the human KLHL11-Cul3 complex at 2.8A resolution · the same entry in another collection · chain A against A, TM-score 1.00
- Q13618 · AlphaFold monomer V2.0 prediction for cullin-3 (Q13618) · a predicted model of the same protein · chain B against A, TM-score 0.98
- Q9NVR0 · AlphaFold monomer V2.0 prediction for kelch-like protein 11 (Q9NVR0) · a predicted model of the same protein · chain A 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 Q9NVR0
- Every structure of UniProt Q13618
- Elsewhere: RCSB PDB 4AP2 · PDBe 4AP2 · UniProt Q9NVR0 · UniProt Q13618
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