Research workbench
Crystal structure of streptomyces coelicolor alpha-L- arabinofuranosidase ethylmercury derivative
Analyse Crystal structure of streptomyces coelicolor alpha-L- arabinofuranosidase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WMZ
- Type
- protein
- Length
- 302 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Extracellular exo-alpha-L-arabinofuranosidase
- EC
- 3.2.1.55
- UniProt
- O54161
- Ligands
- EMC, CA
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Extracellular exo-alpha-L-arabinofuranosidase (EC 3.2.1.55) | protein | 302 | 6% helix, 45% strand | O54161 |
Ligands and binding sites
- EMC · Ethyl mercury ion · ligand · 3 copies · chains A
- CA · Calcium ion · metal · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.49 | 0.82 | 20 | TRS, EMC |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3WMZ · Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase ethylmercury… · the same entry in another collection · chain A against A, TM-score 1.00
- O54161 · AlphaFold monomer V2.0 prediction for extracellular exo-alpha-L- arabinofuranosidase… · 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 O54161
- Elsewhere: RCSB PDB 3WMZ · PDBe 3WMZ · UniProt O54161
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