Research workbench
Crystal Structure of Activin A/BMP2 chimera
Analyse Crystal Structure of Activin A/BMP2 chimera in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MID
- Type
- protein
- Length
- 105 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.139
- Source
- Homo sapiens
- Molecule
- AB204 Activin A/BMP2 chimera
Structure
x-ray diffraction · resolution 2.139 · 1 distinct chain · 18% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | AB204 Activin A/BMP2 chimera | protein | 105 | 18% helix, 45% strand | — |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 4MID · Crystal structure of activin A/BMP2 chimera · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 4MID · PDBe 4MID
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