Research workbench
Crystal structure of protein BAD_0989 from bifidobacterium adolescentis
Analyse Crystal structure of protein BAD_0989 from bifidobacterium adolescentis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CYM
- Type
- protein
- Length
- 415 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein BAD_0989
- UniProt
- A1A237
- Ligands
- NA
- Pockets
- 3 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein BAD_0989 | protein | 415 | 57% helix, 9% strand | A1A237 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 209 | 0.53 | 0.77 | 23 | GOL |
| 2 | 143 | 0.43 | 0.76 | 20 | NA |
| 3 | 87 | 0.32 | 0.73 | 18 | empty |
Compared structures
- 3CYM · Crystal structure of protein BAD_0989 from Bifidobacterium adolescentis · 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 A1A237
- Elsewhere: RCSB PDB 3CYM · PDBe 3CYM · UniProt A1A237
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