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Crystal structure of beta-klotho, domain 1
Analyse Crystal structure of beta-klotho, domain 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5VAK
- Type
- protein
- Length
- 558 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-klotho; NB914
- UniProt
- Q86Z14
- Ligands
- NAG
- Pockets
- 4 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-klotho | protein | 439 | 48% helix, 16% strand | Q86Z14 |
| B | NB914 | protein | 119 | 8% helix, 48% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.47 | 0.80 | 19 | empty |
| 2 | 94 | 0.33 | 0.73 | 17 | empty |
| 3 | 63 | 0.32 | 0.75 | 16 | empty |
| 4 | 61 | 0.30 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 633 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 glycan, 1 disulfide (N-glycosylation, disulfide).
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 Q86Z14
- Elsewhere: RCSB PDB 5VAK · PDBe 5VAK · UniProt Q86Z14
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