MolNFT v1 · #186112 · protein
Crystal structure of the kelch domain of human KBTBD12
7QZQ · Kelch repeat and btb domain-containing protein 12: “Crystal structure of the kelch domain of human KBTBD12”. X-ray diffraction, 1 ligand (NA), 6 pockets (best druggability 0.72). MolNFT v1 #186112 on GenesisL1: 3D structure, binding…
- PDB
- 7QZQ
- Type
- protein
- Length
- 686 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kelch repeat and btb domain-containing protein 12
- UniProt
- Q3ZCT8
- Ligands
- NA
- Pockets
- 6 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kelch repeat and btb domain-containing protein 12 | protein | 344 | 3% helix, 49% strand | Q3ZCT8 |
| B | Kelch repeat and btb domain-containing protein 12 | protein | 342 | 1% helix, 50% strand | Q3ZCT8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 548 | 0.72 | 0.81 | 47 | empty |
| 2 | 425 | 0.71 | 0.82 | 49 | empty |
| 3 | 174 | 0.59 | 0.83 | 34 | EDO |
| 4 | 124 | 0.40 | 0.75 | 27 | empty |
| 5 | 89 | 0.36 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 527 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 7QZQ · Crystal structure of the kelch domain of human KBTBD12 · the same entry in another collection · chain A against A, TM-score 1.00
- Q3ZCT8 · AlphaFold monomer V2.0 prediction for kelch repeat and btb domain- containing protein 12… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q3ZCT8
- Elsewhere: RCSB PDB 7QZQ · PDBe 7QZQ · UniProt Q3ZCT8
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