Research workbench
The crystal structure of a single chain H2B-H2A histone chimera from xenopus laevis
Analyse The crystal structure of a single chain H2B-H2A histone chimera from xenopus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6W4L
- Type
- protein
- Length
- 176 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone H2B 1.1,HISTONE H2A type 1
- UniProt
- P02281, P06897
- Ligands
- PPV
Structure
x-ray diffraction · 1 distinct chain · 72% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone H2B 1.1,HISTONE H2A type 1 | protein | 176 | 72% helix, 5% strand | P02281, P06897 |
Ligands and binding sites
- PPV · Pyrophosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6W4L · The crystal structure of a single chain H2B-H2A histone chimera from Xenopus laevis · the same entry in another collection · chain A against A, TM-score 1.00
- P06897 · AlphaFold monomer V2.0 prediction for histone H2A type 1 (P06897) · a predicted model of the same protein · chain A against A, TM-score 0.47
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 P02281
- Every structure of UniProt P06897
- Elsewhere: RCSB PDB 6W4L · PDBe 6W4L · UniProt P02281 · UniProt P06897
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