Research workbench
Solution structure of LEDGF/P75 ibd in complex with MLL1 peptide (140- 160)
Analyse Solution structure of LEDGF/P75 ibd in complex with MLL1 peptide (140- 160) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MSR
- Type
- protein
- Length
- 109 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-lysine N-methyltransferase 2A; PC4 and SFRS1-interacting protein
- UniProt
- Q03164, O75475
Structure
solution nmr · 2 distinct chains · 54% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase 2A | protein | 21 | 0% helix, 0% strand | Q03164 |
| B | PC4 and SFRS1-interacting protein | protein | 88 | 67% helix, 2% strand | O75475 |
Interfaces
1 interface between chains.
- A–B · 303 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2MSR · Solution structure of LEDGF/p75 IBD in complex with MLL1 peptide (140-160) · the same entry in another collection · chain A against A, TM-score 1.00
- O75475 · AlphaFold monomer V2.0 prediction for PC4 and SFRS1-interacting protein (O75475) · a predicted model of the same protein · chain B against A, TM-score 0.87
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 Q03164
- Every structure of UniProt O75475
- Elsewhere: RCSB PDB 2MSR · PDBe 2MSR · UniProt Q03164 · UniProt O75475
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.