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Crystal structure of exo-1,3/1,4-beta-glucanase (exop) from pseudoalteromonas sp. BB1
Analyse Crystal structure of exo-1,3/1,4-beta-glucanase (exop) from pseudoalteromonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UT0
- Type
- protein
- Length
- 3,199 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Exo-1,3/1,4-beta-glucanase
- EC
- 3.2.1.-
- UniProt
- Q0QJA3
- Ligands
- CA, NA, SO4
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 3 distinct chains · 31% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Exo-1,3/1,4-beta-glucanase (EC 3.2.1.-) | protein | 804 | 31% helix, 23% strand | Q0QJA3 |
| B, C | Exo-1,3/1,4-beta-glucanase (EC 3.2.1.-) | protein | 798 | 31% helix, 23% strand | Q0QJA3 |
| D | Exo-1,3/1,4-beta-glucanase (EC 3.2.1.-) | protein | 799 | 31% helix, 23% strand | Q0QJA3 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A, B, C, D
- NA · Sodium ion · metal · 4 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 18 copies · chains A, B, C, D
- EDO · 1,2-ethanediol · additive · 9 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1003 | 0.78 | 0.80 | 96 | empty |
| 2 | 1062 | 0.76 | 0.79 | 118 | EDO |
| 3 | 1017 | 0.75 | 0.78 | 104 | EDO |
| 4 | 402 | 0.65 | 0.79 | 42 | empty |
| 5 | 163 | 0.62 | 0.84 | 32 | empty |
Interfaces
4 interfaces between chains.
- A–B · 585 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 513 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 399 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 368 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 3UT0 · Crystal structure of exo-1,3/1,4-beta-glucanase (EXOP) from Pseudoalteromonas sp. BB1 · 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 Q0QJA3
- Elsewhere: RCSB PDB 3UT0 · PDBe 3UT0 · UniProt Q0QJA3
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