Research workbench
Structure of hormoconis resinae glucoamylase
Analyse Structure of hormoconis resinae glucoamylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FHW
- Type
- protein
- Length
- 1,173 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucoamylase P
- EC
- 3.2.1.3
- UniProt
- Q03045
- Ligands
- AC1, NAG, GLC, MAN, BMA
- Pockets
- 8 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucoamylase P (EC 3.2.1.3) | protein | 586 | 38% helix, 13% strand | Q03045 |
| B | Glucoamylase P (EC 3.2.1.3) | protein | 587 | 38% helix, 13% strand | Q03045 |
Ligands and binding sites
- AC1 · 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose · ligand · 2 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 22 copies · chains A, B
- GLC · alpha-D-glucopyranose · sugar · 4 copies · chains A, B
- MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A
- BMA · beta-D-mannopyranose · sugar
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.72 | 0.97 | 26 | empty |
| 2 | 103 | 0.72 | 0.94 | 33 | empty |
| 3 | 312 | 0.60 | 0.78 | 40 | GLC, AC1 |
| 4 | 97 | 0.55 | 0.84 | 19 | GLC, AC1 |
| 5 | 269 | 0.54 | 0.76 | 53 | empty |
Interfaces
1 interface between chains.
- A–B · 497 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 glycan, 10 disulfide (N-glycosylation, disulfide).
Compared structures
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 Q03045
- Elsewhere: RCSB PDB 6FHW · PDBe 6FHW · UniProt Q03045
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