Research workbench
Crystal structure of maf-like protein BCEJ2315_23540 from burkholderia cenocepacia
Analyse Crystal structure of maf-like protein BCEJ2315_23540 from burkholderia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OO0
- Type
- protein
- Length
- 412 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maf-like protein BCAL2394
- UniProt
- B4E5S2
- Ligands
- PO4
- Pockets
- 5 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maf-like protein BCAL2394 | protein | 208 | 38% helix, 23% strand | B4E5S2 |
| B | Maf-like protein BCAL2394 | protein | 204 | 39% helix, 25% strand | B4E5S2 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 8 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 71 | 0.66 | 0.93 | 23 | PO4 |
| 2 | 229 | 0.65 | 0.83 | 40 | PO4, EDO |
| 3 | 336 | 0.63 | 0.79 | 41 | PO4, EDO |
| 4 | 96 | 0.60 | 0.87 | 23 | PO4 |
| 5 | 252 | 0.54 | 0.76 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 1094 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 4OO0 · Crystal Structure of Maf-like protein BceJ2315_23540 from Burkholderia cenocepacia · 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 B4E5S2
- Elsewhere: RCSB PDB 4OO0 · PDBe 4OO0 · UniProt B4E5S2
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