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Crystal structure of the laminarinase catalytic domain from thermotoga maritima MSB8
Analyse Crystal structure of the laminarinase catalytic domain from thermotoga maritima… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AZY
- Type
- protein
- Length
- 1,004 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Laminarinase
- EC
- 3.2.1.39
- UniProt
- Q9WXN1
- Ligands
- CA, SO4
- Pockets
- 10 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Laminarinase (EC 3.2.1.39) | protein | 251 | 8% helix, 48% strand | Q9WXN1 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 12 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 302 | 0.64 | 0.80 | 39 | SO4 |
| 2 | 281 | 0.64 | 0.81 | 35 | SO4 |
| 3 | 594 | 0.64 | 0.75 | 56 | empty |
| 4 | 298 | 0.63 | 0.80 | 36 | SO4 |
| 5 | 545 | 0.63 | 0.75 | 58 | empty |
Interfaces
5 interfaces between chains.
- C–D · 476 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 468 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 452 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 422 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 291 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 3AZY · Crystal structure of the laminarinase catalytic domain from Thermotoga maritima MSB8 · 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 Q9WXN1
- Elsewhere: RCSB PDB 3AZY · PDBe 3AZY · UniProt Q9WXN1
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