Research workbench
Crystal structure of an enolase from the soil bacterium cellvibrio japonicus (target efi-502161) with bound mg and glycerol
Analyse Crystal structure of an enolase from the soil bacterium cellvibrio japonicus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3V3W
- Type
- protein
- Length
- 397 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Starvation sensing protein rspa
- UniProt
- B3PDB1
- Ligands
- MG, CL
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Starvation sensing protein rspa | protein | 397 | 38% helix, 20% strand | B3PDB1 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- NHE · 2-[N-cyclohexylamino]ethane sulfonic acid · additive · 2 copies · chains A
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 | 385 | 0.64 | 0.79 | 43 | GOL |
| 2 | 109 | 0.37 | 0.74 | 19 | empty |
Compared structures
- 3V3W · Crystal structure of an enolase from the soil bacterium Cellvibrio japonicus (TARGET… · the same entry in another collection · chain A against A, TM-score 1.00
- B3PDB1 · AlphaFold monomer V2.0 prediction for D-galactonate dehydratase family member rspa… · a predicted model of the same protein · 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 B3PDB1
- Elsewhere: RCSB PDB 3V3W · PDBe 3V3W · UniProt B3PDB1
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