Research workbench
Structure of the cmgc cdk kinase from giardia lamblia in complex with AMP
Analyse Structure of the cmgc cdk kinase from giardia lamblia in complex with AMP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GC0
- Type
- protein
- Length
- 278 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kinase, cmgc cdk
- UniProt
- A8BZ95
- Ligands
- AMP
- Pockets
- 4 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kinase, cmgc cdk | protein | 278 | 42% helix, 18% strand | A8BZ95 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 214 | 0.56 | 0.79 | 33 | AMP |
| 2 | 78 | 0.36 | 0.76 | 20 | empty |
| 3 | 51 | 0.34 | 0.78 | 15 | empty |
| 4 | 59 | 0.29 | 0.74 | 16 | empty |
Compared structures
- 3GC0 · Structure of the CMGC CDK Kinase from Giardia lamblia in complex with AMP · 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 A8BZ95
- Elsewhere: RCSB PDB 3GC0 · PDBe 3GC0 · UniProt A8BZ95
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