Research workbench
Novel GH12 endogluconase from aspergillus cervinus
Analyse Novel GH12 endogluconase from aspergillus cervinus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7P1Z
- Type
- protein
- Length
- 672 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycoside hydrolase
- Ligands
- K
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 3 distinct chains · 9% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Glycoside hydrolase | protein | 223 | 9% helix, 57% strand | — |
| C | Glycoside hydrolase | protein | 226 | 9% helix, 55% strand | — |
| A | Glycoside hydrolase | protein | 223 | 9% helix, 56% strand | — |
Ligands and binding sites
- K · Potassium ion · metal · chains A
- ACT · Acetate ion · additive · 6 copies · chains B, C, A
- PEG · Di(hydroxyethyl)ether · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 949 | 0.74 | 0.78 | 98 | empty |
| 2 | 303 | 0.72 | 0.85 | 45 | empty |
| 3 | 186 | 0.46 | 0.75 | 33 | PEG |
Interfaces
3 interfaces between chains.
- C–A · 554 Ų buried · 6 hydrogen bonds · protein-protein
- B–A · 353 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 100 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 7P1Z · Novel GH12 endogluconase from Aspergillus cervinus · the same entry in another collection · chain B against B, 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
- Elsewhere: RCSB PDB 7P1Z · PDBe 7P1Z
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