Research workbench
Crystal structure of the extracellular domain of the type II bmp receptor
Analyse Crystal structure of the extracellular domain of the type II bmp receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HLQ
- Type
- protein
- Length
- 100 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bone morphogenetic protein receptor type-2
- EC
- 2.7.11.30
- UniProt
- Q4ZG08
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bone morphogenetic protein receptor type-2 (EC 2.7.11.30) | protein | 100 | 10% helix, 36% strand | Q4ZG08 |
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 2HLQ · Crystal Structure of the Extracellular Domain of the Type II BMP Receptor · 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
- Every structure of UniProt Q4ZG08
- Elsewhere: RCSB PDB 2HLQ · PDBe 2HLQ · UniProt Q4ZG08
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