MolNFT v1 · #32894 · protein
Structure of CBM25 from bacillus halodurans amylase in complex with maltotetraose
2C3W · Alpha-amylase G-6: “Structure of CBM25 from bacillus halodurans amylase in complex with maltotetraose”. X-ray diffraction, 2 ligands (GLC, SO4), 3 pockets (best druggability 0.64). MolNFT v1 #32894 on GenesisL1: 3D structure…
- PDB
- 2C3W
- Type
- protein
- Length
- 378 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-amylase G-6
- UniProt
- Q9KFR4
- Ligands
- GLC, SO4
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Alpha-amylase G-6 | protein | 95 | 0% helix, 48% strand | Q9KFR4 |
| D | Alpha-amylase G-6 | protein | 93 | 0% helix, 49% strand | Q9KFR4 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 35 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 590 | 0.64 | 0.75 | 71 | GLC |
| 2 | 219 | 0.47 | 0.74 | 33 | GLC |
| 3 | 98 | 0.31 | 0.72 | 22 | empty |
Interfaces
5 interfaces between chains.
- A–D · 267 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 237 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 210 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 190 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 63 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2C3W · Structure of CBM25 from Bacillus halodurans amylase in complex with maltotetraose · 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 Q9KFR4
- Elsewhere: RCSB PDB 2C3W · PDBe 2C3W · UniProt Q9KFR4
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