Research workbench
Crystal structure of human brm in complex with compound 15
Analyse Crystal structure of human brm in complex with compound 15 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EG3
- Type
- protein
- Length
- 614 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MALTOSE/MALTODEXTRIN-binding periplasmic PROTEIN,PROBABLE global transcription activator…
- EC
- 3.6.4.-
- UniProt
- P0AEY0, P51531
- Ligands
- J7G
- Pockets
- 4 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MALTOSE/MALTODEXTRIN-binding periplasmic PROTEIN,PROBABLE global transcription activator SNF2L2 (EC 3.6.4.-) | protein | 614 | 47% helix, 16% strand | P0AEY0, P51531 |
Ligands and binding sites
- J7G · 3-[(4-{[(2-chloropyridin-4-yl)carbamoyl]amino}pyridin-2-yl)ethynyl]benzoic acid · ligand · chains A
- EOH · Ethanol · additive · 6 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 160 | 0.70 | 0.89 | 29 | J7G |
| 2 | 585 | 0.62 | 0.74 | 66 | EOH |
| 3 | 136 | 0.54 | 0.81 | 31 | EOH |
| 4 | 59 | 0.30 | 0.74 | 15 | EOH |
Compared structures
- 6EG3 · Crystal structure of human BRM in complex with compound 15 · the same entry in another collection · chain A against A, TM-score 1.00
- P51531 · AlphaFold monomer V2.0 prediction for probable global transcription activator SNF2L2… · a predicted model of the same protein · chain A against A, TM-score 0.42
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 P0AEY0
- Every structure of UniProt P51531
- Elsewhere: RCSB PDB 6EG3 · PDBe 6EG3 · UniProt P0AEY0 · UniProt P51531
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