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Crystal structure of human cyclin B1
Analyse Crystal structure of human cyclin B1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2B9R
- Type
- protein
- Length
- 509 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human cyclin B1
- UniProt
- P14635
- Pockets
- 6 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 61% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Human cyclin B1 | protein | 254 | 59% helix, 0% strand | P14635 |
| B | Human cyclin B1 | protein | 255 | 64% helix, 0% strand | P14635 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 130 | 0.79 | 0.96 | 24 | empty |
| 2 | 112 | 0.79 | 0.98 | 23 | empty |
| 3 | 53 | 0.35 | 0.79 | 17 | empty |
| 4 | 55 | 0.33 | 0.78 | 12 | empty |
| 5 | 59 | 0.32 | 0.76 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 889 Ų buried · 17 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 P14635
- Elsewhere: RCSB PDB 2B9R · PDBe 2B9R · UniProt P14635
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