Research workbench
Crystal structure of human pro-myostatin precursor at 4.2 a resolution with experimental phases from semet labelling
Analyse Crystal structure of human pro-myostatin precursor at 4.2 a resolution with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NXS
- Type
- protein
- Length
- 541 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GROWTH/DIFFERENTIATION factor 8
- UniProt
- O14793
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 16% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GROWTH/DIFFERENTIATION factor 8 | protein | 290 | 16% helix, 33% strand | O14793 |
| B | GROWTH/DIFFERENTIATION factor 8 | protein | 251 | 17% helix, 35% strand | O14793 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 590 | 0.74 | 0.81 | 73 | empty |
| 2 | 868 | 0.72 | 0.76 | 74 | empty |
| 3 | 202 | 0.55 | 0.79 | 35 | empty |
| 4 | 81 | 0.42 | 0.79 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1969 Ų buried · 25 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide, 10 modified (disulfide, engineered).
Compared structures
- 5NXS · Crystal Structure of Human Pro-myostatin Precursor at 4.2 A Resolution with Experimental… · 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 0.78
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 5NXS · PDBe 5NXS · UniProt O14793
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