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Crystal structure of human brain-type creatine kinase
Analyse Crystal structure of human brain-type creatine kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DRB
- Type
- protein
- Length
- 752 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Creatine kinase B-type
- EC
- 2.7.3.2
- UniProt
- P12277
- Ligands
- ADP, MG
- Pockets
- 4 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Creatine kinase B-type (EC 2.7.3.2) | protein | 376 | 39% helix, 17% strand | P12277 |
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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 709 | 0.80 | 0.84 | 79 | MG, ADP |
| 2 | 396 | 0.71 | 0.83 | 54 | empty |
| 3 | 751 | 0.67 | 0.75 | 74 | empty |
| 4 | 86 | 0.35 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 571 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
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 P12277
- Elsewhere: RCSB PDB 3DRB · PDBe 3DRB · UniProt P12277
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