Research workbench
human Myeloid-derived growth factor (MYDGF)
Analyse human Myeloid-derived growth factor (MYDGF) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SVK
- Type
- protein
- Length
- 271 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.604
- Source
- Homo sapiens
- Molecule
- Myeloid-derived growth factor
- UniProt
- Q969H8
- Pockets
- 2 · best druggability 0.77
Structure
x-ray diffraction · resolution 1.604 · 2 distinct chains · 3% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myeloid-derived growth factor | protein | 135 | 4% helix, 56% strand | Q969H8 |
| B | Myeloid-derived growth factor | protein | 136 | 2% helix, 55% strand | Q969H8 |
Ligands and binding sites
- MLI · Malonate ion · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 636 | 0.77 | 0.83 | 61 | empty |
| 2 | 180 | 0.48 | 0.76 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 933 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (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 Q969H8
- Elsewhere: RCSB PDB 6SVK · PDBe 6SVK · UniProt Q969H8
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