Research workbench
Crystal structure of protein BH3703 from bacillus halodurans, pfam DUF600
Analyse Crystal structure of protein BH3703 from bacillus halodurans, pfam DUF600 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IA1
- Type
- protein
- Length
- 339 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BH3703 protein
- UniProt
- Q9K6M5
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BH3703 protein | protein | 169 | 49% helix, 21% strand | Q9K6M5 |
| B | BH3703 protein | protein | 170 | 48% helix, 21% strand | Q9K6M5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 243 | 0.58 | 0.79 | 35 | empty |
| 2 | 59 | 0.35 | 0.77 | 14 | SO4 |
Interfaces
1 interface between chains.
- A–B · 1234 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 2IA1 · Crystal structure of protein BH3703 from Bacillus halodurans, Pfam DUF600 · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9K6M5
- Elsewhere: RCSB PDB 2IA1 · PDBe 2IA1 · UniProt Q9K6M5
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