Research workbench
Ruminococcus bromii AMY12-D392A with 63-a-D-glucosyl-maltotriose
Analyse Ruminococcus bromii AMY12-D392A with 63-a-D-glucosyl-maltotriose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LSU
- Type
- protein
- Length
- 765 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pullulanase
- EC
- 3.2.1.41
- UniProt
- A0A2N0UU23
- Ligands
- GLC, BGC, CA, NA
- Pockets
- 9 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pullulanase (EC 3.2.1.41) | protein | 765 | 25% helix, 27% strand | A0A2N0UU23 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 3 copies · chains A
- BGC · beta-D-glucopyranose · sugar · chains A
- CA · Calcium ion · metal · chains A
- NA · Sodium ion · metal · chains A
- GOL · Glycerol · additive · 7 copies · chains A
- ACT · Acetate ion · additive · 7 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 109 | 0.69 | 0.91 | 21 | empty |
| 2 | 157 | 0.63 | 0.85 | 35 | GOL |
| 3 | 258 | 0.57 | 0.78 | 32 | BGC, GLC, GOL |
| 4 | 188 | 0.53 | 0.79 | 29 | GOL |
| 5 | 103 | 0.45 | 0.79 | 23 | empty |
Compared structures
- 7LSU · Ruminococcus bromii Amy12-D392A with 63-a-D-glucosyl-maltotriose · 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 A0A2N0UU23
- Elsewhere: RCSB PDB 7LSU · PDBe 7LSU · UniProt A0A2N0UU23
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