Research workbench
Crystal structure of human pro-myostatin precursor at 2.6 a resolution
Analyse Crystal structure of human pro-myostatin precursor at 2.6 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NTU
- Type
- protein
- Length
- 581 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GROWTH/DIFFERENTIATION factor 8
- UniProt
- O14793
- Ligands
- CL
- Pockets
- 6 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 16% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GROWTH/DIFFERENTIATION factor 8 | protein | 308 | 15% helix, 39% strand | O14793 |
| B | GROWTH/DIFFERENTIATION factor 8 | protein | 273 | 17% helix, 39% strand | O14793 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 21 copies · chains A, B
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 | 933 | 0.74 | 0.77 | 91 | EDO |
| 2 | 389 | 0.70 | 0.82 | 44 | empty |
| 3 | 168 | 0.52 | 0.79 | 25 | EDO |
| 4 | 52 | 0.33 | 0.78 | 19 | empty |
| 5 | 61 | 0.29 | 0.74 | 12 | EDO |
Interfaces
1 interface between chains.
- A–B · 3020 Ų buried · 37 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 disulfide (disulfide).
Compared structures
- 5NTU · Crystal Structure of human Pro-myostatin Precursor at 2.6 A Resolution · the same entry in another collection · chain A against A, TM-score 1.00
- O14793 · AlphaFold monomer V2.0 prediction for GROWTH/DIFFERENTIATION factor 8 (O14793) · 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 O14793
- Elsewhere: RCSB PDB 5NTU · PDBe 5NTU · UniProt O14793
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