Research workbench
Crystal structure of PHC3 SAM L971E
Analyse Crystal structure of PHC3 SAM L971E in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PZN
- Type
- protein
- Length
- 345 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polyhomeotic-like protein 3
- UniProt
- Q8NDX5
Structure
x-ray diffraction · 4 distinct chains · 64% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyhomeotic-like protein 3 | protein | 70 | 64% helix, 0% strand | Q8NDX5 |
| B, D | Polyhomeotic-like protein 3 | protein | 69 | 62% helix, 0% strand | Q8NDX5 |
| C | Polyhomeotic-like protein 3 | protein | 70 | 66% helix, 0% strand | Q8NDX5 |
| E | Polyhomeotic-like protein 3 | protein | 67 | 64% helix, 0% strand | Q8NDX5 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 5 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
4 interfaces between chains.
- B–D · 519 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 484 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 483 Ų buried · 8 hydrogen bonds · protein-protein
- D–E · 454 Ų buried · 5 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 Q8NDX5
- Elsewhere: RCSB PDB 4PZN · PDBe 4PZN · UniProt Q8NDX5
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