Research workbench
Crystal structure of kinesin-like calmodulin binding protein
Analyse Crystal structure of kinesin-like calmodulin binding protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SDM
- Type
- protein
- Length
- 344 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kinesin heavy chain-like protein
- UniProt
- Q41460
- Ligands
- ADP, MG
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kinesin heavy chain-like protein | protein | 344 | 31% helix, 27% strand | Q41460 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 334 | 0.57 | 0.76 | 39 | MG, ADP |
| 2 | 256 | 0.52 | 0.75 | 28 | empty |
| 3 | 88 | 0.38 | 0.76 | 17 | empty |
| 4 | 57 | 0.34 | 0.78 | 14 | empty |
Compared structures
- 1SDM · Crystal structure of kinesin-like calmodulin binding protein · 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 Q41460
- Elsewhere: RCSB PDB 1SDM · PDBe 1SDM · UniProt Q41460
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