Research workbench
Crystal structure of the BRMS1 N-terminal region
Analyse Crystal structure of the BRMS1 N-terminal region in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AUV
- Type
- protein
- Length
- 208 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Breast cancer metastasis suppressor 1
- UniProt
- Q9HCU9
- Ligands
- CL, SO4
- Pockets
- 2 · best druggability 0.37
Structure
x-ray diffraction · 6 distinct chains · 86% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Breast cancer metastasis suppressor 1 | protein | 35 | 89% helix, 0% strand | Q9HCU9 |
| B, G | Breast cancer metastasis suppressor 1 | protein | 27 | 85% helix, 0% strand | Q9HCU9 |
| D | Breast cancer metastasis suppressor 1 | protein | 18 | 89% helix, 0% strand | Q9HCU9 |
| E | Breast cancer metastasis suppressor 1 | protein | 21 | 81% helix, 0% strand | Q9HCU9 |
| F | Breast cancer metastasis suppressor 1 | protein | 23 | 91% helix, 0% strand | Q9HCU9 |
| H | Breast cancer metastasis suppressor 1 | protein | 22 | 82% helix, 0% strand | Q9HCU9 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
- SO4 · Sulfate ion · ion · chains A, B
- ACY · Acetic acid · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 76 | 0.37 | 0.76 | 12 | empty |
| 2 | 51 | 0.34 | 0.78 | 12 | empty |
Interfaces
16 interfaces between chains.
- C–H · 466 Ų buried · 2 hydrogen bonds · protein-protein
- F–G · 446 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 440 Ų buried · 3 hydrogen bonds · protein-protein
- B–E · 409 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 334 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 Q9HCU9
- Elsewhere: RCSB PDB 4AUV · PDBe 4AUV · UniProt Q9HCU9
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