Research workbench
Crystal structure of chicken brain-type creatine kinase at 1.41 ångström resolution
Analyse Crystal structure of chicken brain-type creatine kinase at 1.41 ångström… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QH4
- Type
- protein
- Length
- 1,520 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Creatine kinase
- EC
- 2.7.3.2
- UniProt
- P05122
- Ligands
- CA
- Pockets
- 15 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Creatine kinase (EC 2.7.3.2) | protein | 380 | 39% helix, 16% strand | P05122 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.76 | 0.98 | 27 | empty |
| 2 | 94 | 0.75 | 0.97 | 29 | empty |
| 3 | 603 | 0.69 | 0.78 | 62 | ACT |
| 4 | 444 | 0.64 | 0.77 | 48 | ACT |
| 5 | 408 | 0.62 | 0.77 | 34 | empty |
Interfaces
2 interfaces between chains.
- C–D · 1872 Ų buried · 49 hydrogen bonds · protein-protein
- A–B · 1841 Ų buried · 47 hydrogen bonds · protein-protein
Compared structures
- 1QH4 · Crystal structure of chicken brain-type creatine kinase at 1.41 ångström resolution · the same entry in another collection · chain A against A, TM-score 1.00
- P05122 · AlphaFold monomer V2.0 prediction for creatine kinase B-type (P05122) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P05122
- Elsewhere: RCSB PDB 1QH4 · PDBe 1QH4 · UniProt P05122
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