Research workbench
DNA-binding domain of human setmar in complex with HSMAR1 terminal inverted repeat (tir) DNA
Analyse DNA-binding domain of human setmar in complex with HSMAR1 terminal inverted… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7S03
- Type
- protein + DNA
- Length
- 160 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-lysine N-methyltransferase setmar; HSMAR1 terminal inverted repeats
- EC
- 2.1.1.357, 3.1.-.-
- UniProt
- Q53H47
- Pockets
- 1 · best druggability 0.42
Structure
x-ray diffraction · 3 distinct chains · 60% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase setmar (EC 2.1.1.357, 3.1.-.-) | protein | 108 | 60% helix, 0% strand | Q53H47 |
| B | HSMAR1 terminal inverted repeats | dna | 26 | — | — |
| C | HSMAR1 terminal inverted repeats | dna | 26 | — | — |
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 | 123 | 0.42 | 0.77 | 22 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1160 Ų buried · 103 hydrogen bonds · nucleic-nucleic
- A–C · 1109 Ų buried · 22 hydrogen bonds · protein-nucleic
- A–B · 1013 Ų buried · 17 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 7S03 · DNA-binding domain of human SETMAR in complex with Hsmar1 terminal inverted repeat (TIR)… · the same entry in another collection · chain A against A, TM-score 1.00
- Q53H47 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase setmar (Q53H47) · a predicted model of the same protein · chain A against A, TM-score 0.85
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 Q53H47
- Elsewhere: RCSB PDB 7S03 · PDBe 7S03 · UniProt Q53H47
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