Research workbench
Crystal structure of the dimerization domain of human cenp-B
Analyse Crystal structure of the dimerization domain of human cenp-B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UFI
- Type
- protein
- Length
- 188 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major centromere autoantigen B
- UniProt
- P07199
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 4 distinct chains · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Major centromere autoantigen B | protein | 48 | 73% helix, 0% strand | P07199 |
| B | Major centromere autoantigen B | protein | 46 | 78% helix, 0% strand | P07199 |
| C | Major centromere autoantigen B | protein | 48 | 71% helix, 0% strand | P07199 |
| D | Major centromere autoantigen B | protein | 46 | 74% helix, 0% strand | P07199 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 86 | 0.40 | 0.78 | 18 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1427 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 1366 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 323 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 267 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 158 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1UFI · Crystal structure of the dimerization domain of human CENP-B · the same entry in another collection · chain D against D, TM-score 1.00
- P07199 · AlphaFold monomer V2.0 prediction for major centromere autoantigen B (P07199) · a predicted model of the same protein · chain B against A, TM-score 0.86
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 P07199
- Elsewhere: RCSB PDB 1UFI · PDBe 1UFI · UniProt P07199
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