Research workbench
Human BMP6 homodimer
Analyse Human BMP6 homodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OMO
- Type
- protein
- Length
- 208 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bone morphogenetic protein 6
- UniProt
- P22004
- Ligands
- NAG
- Pockets
- 3 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| I, J | Bone morphogenetic protein 6 | protein | 104 | 18% helix, 45% strand | P22004 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains J, I
- IPA · Isopropyl alcohol · additive · 6 copies · chains I, J
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains I, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 66 | 0.44 | 0.81 | 14 | PEG |
| 2 | 143 | 0.43 | 0.75 | 30 | empty |
| 3 | 64 | 0.27 | 0.73 | 21 | empty |
Interfaces
1 interface between chains.
- I–J · 1219 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 disulfide, 2 glycan (disulfide, N-glycosylation).
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 P22004
- Elsewhere: RCSB PDB 6OMO · PDBe 6OMO · UniProt P22004
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