Research workbench
Smooth muscle myosin motor domain-essential light chain complex with MGADP.BEF3 bound at the active site
Analyse Smooth muscle myosin motor domain-essential light chain complex with MGADP.BEF3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BR4
- Type
- protein
- Length
- 3,716 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P10587, P02607
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G | — | protein | 781 | — | P10587 |
| B, D, F, H | — | protein | 148 | — | P02607 |
Compared structures
- 1BR4 · Smooth muscle myosin motor domain-essential light chain complex with MGADP.BEF3 bound at… · 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 P10587
- Every structure of UniProt P02607
- Elsewhere: RCSB PDB 1BR4 · PDBe 1BR4 · UniProt P10587 · UniProt P02607
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