Research workbench
Benm effector binding domain- semet derivative
Analyse Benm effector binding domain- semet derivative in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F6P
- Type
- protein
- Length
- 442 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hth-type transcriptional regulator benm
- UniProt
- O68014
- Ligands
- NA, SO4
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hth-type transcriptional regulator benm | protein | 218 | 33% helix, 28% strand | O68014 |
| B | Hth-type transcriptional regulator benm | protein | 224 | 34% helix, 27% strand | O68014 |
Ligands and binding sites
- NA · Sodium ion · metal · chains B
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
- ACT · Acetate ion · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 318 | 0.67 | 0.81 | 41 | empty |
| 2 | 154 | 0.55 | 0.81 | 25 | SO4 |
Interfaces
1 interface between chains.
- A–B · 1318 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
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 O68014
- Elsewhere: RCSB PDB 2F6P · PDBe 2F6P · UniProt O68014
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