Research workbench
Hetero SAM domain structure of pH and scm.
Analyse Hetero SAM domain structure of pH and scm. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PK1
- Type
- protein
- Length
- 271 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polyhomeotic-proximal chromatin protein; Sex comb on midleg CG9495-pa
- UniProt
- P39769, Q9VHA0
Structure
x-ray diffraction · 4 distinct chains · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyhomeotic-proximal chromatin protein | protein | 68 | 65% helix, 0% strand | P39769 |
| B | Sex comb on midleg CG9495-pa | protein | 70 | 74% helix, 0% strand | Q9VHA0 |
| C | Polyhomeotic-proximal chromatin protein | protein | 66 | 70% helix, 0% strand | P39769 |
| D | Sex comb on midleg CG9495-pa | protein | 67 | 72% helix, 0% strand | Q9VHA0 |
Interfaces
3 interfaces between chains.
- A–C · 563 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 504 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 492 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified, 1 disulfide (engineered, disulfide).
Compared structures
- 1PK1 · Hetero SAM domain structure of Ph and Scm. · the same entry in another collection · chain D against D, TM-score 1.00
- Q9VHA0 · AlphaFold monomer V2.0 prediction for polycomb protein scm (Q9VHA0) · a predicted model of the same protein · chain B against A, TM-score 0.98
- P39769 · AlphaFold monomer V2.0 prediction for polyhomeotic-proximal chromatin protein (P39769) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P39769
- Every structure of UniProt Q9VHA0
- Elsewhere: RCSB PDB 1PK1 · PDBe 1PK1 · UniProt P39769 · UniProt Q9VHA0
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