Research workbench
Structural and functional characterisation of the kindlin-1 pleckstrin homology domain
Analyse Structural and functional characterisation of the kindlin-1 pleckstrin homology… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BBK
- Type
- protein
- Length
- 121 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fermitin family homolog 1
- UniProt
- E9Q7J9
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fermitin family homolog 1 | protein | 121 | 27% helix, 42% strand | E9Q7J9 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4BBK · Structural and functional characterisation of the kindlin-1 pleckstrin homology domain · 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 E9Q7J9
- Elsewhere: RCSB PDB 4BBK · PDBe 4BBK · UniProt E9Q7J9
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