Research workbench
Structural basis of histone H2A-H2B recognition by the essential chaperone fact
Analyse Structural basis of histone H2A-H2B recognition by the essential chaperone fact in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KHA
- Type
- protein
- Length
- 452 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SPT16M-histone H2B 1.1 chimera; Histone H2A
- UniProt
- G0SDN1, P02281, Q6AZJ8
- Ligands
- CL
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SPT16M-histone H2B 1.1 chimera | protein | 360 | 38% helix, 29% strand | G0SDN1, P02281 |
| B | Histone H2A | protein | 92 | 63% helix, 4% strand | Q6AZJ8 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 2546 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 4KHA · Structural basis of histone H2A-H2B recognition by the essential chaperone FACT · 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 G0SDN1
- Every structure of UniProt P02281
- Every structure of UniProt Q6AZJ8
- Elsewhere: RCSB PDB 4KHA · PDBe 4KHA · UniProt G0SDN1 · UniProt P02281 · UniProt Q6AZJ8
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