Research workbench
The conserved candida albicans CA3427 gene product defines a new family of proteins exhibiting the generic periplasmic binding protein structural fold
Analyse The conserved candida albicans CA3427 gene product defines a new family of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2X7P
- Type
- protein
- Length
- 306 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Possible thiamine biosynthesis enzyme
- UniProt
- Q59X88
- Ligands
- AE3, CA, CL, CO2
- Pockets
- 1 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Possible thiamine biosynthesis enzyme | protein | 306 | 43% helix, 18% strand | Q59X88 |
Ligands and binding sites
- AE3 · 2-(2-ethoxyethoxy)ethanol · ligand · chains A
- CA · Calcium ion · metal · chains A
- CL · Chloride ion · ion · chains A
- CO2 · Carbon dioxide · ion · chains A
- ACY · Acetic acid · additive · 5 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 437 | 0.66 | 0.78 | 41 | AE3, ACY, CO2 |
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 2X7P · The Conserved Candida albicans CA3427 Gene Product Defines a New Family of Proteins… · 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 Q59X88
- Elsewhere: RCSB PDB 2X7P · PDBe 2X7P · UniProt Q59X88
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