Research workbench
Catalytic domain of beta-agarase from microbulbifer thermotolerans jamb-A94
Analyse Catalytic domain of beta-agarase from microbulbifer thermotolerans jamb-A94 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WZ1
- Type
- protein
- Length
- 277 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Agarase
- EC
- 3.2.1.81
- UniProt
- Q6F4N4
- Ligands
- NA
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Agarase (EC 3.2.1.81) | protein | 277 | 11% helix, 40% strand | Q6F4N4 |
Ligands and binding sites
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 | 207 | 0.56 | 0.79 | 26 | GOL |
Compared structures
- 3WZ1 · Catalytic domain of beta-agarase from Microbulbifer thermotolerans JAMB-A94 · 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 Q6F4N4
- Elsewhere: RCSB PDB 3WZ1 · PDBe 3WZ1 · UniProt Q6F4N4
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