Research workbench
Hinge-bending motion of D-allose binding protein from escherichia COLI: three open conformations
Analyse Hinge-bending motion of D-allose binding protein from escherichia COLI: three… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GUD
- Type
- protein
- Length
- 576 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D-allose-binding periplasmic protein
- UniProt
- P39265
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | D-allose-binding periplasmic protein | protein | 288 | 45% helix, 21% strand | P39265 |
Ligands and binding sites
- ZN · Zinc ion · metal · 8 copies · chains A, B
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 | 459 | 0.62 | 0.76 | 59 | empty |
| 2 | 289 | 0.59 | 0.78 | 46 | empty |
| 3 | 187 | 0.45 | 0.74 | 33 | empty |
Interfaces
1 interface between chains.
- A–B · 701 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 1GUD · Hinge-bending motion of D-allose binding protein from Escherichia coli: three open… · the same entry in another collection · chain A against A, TM-score 1.00
- P39265 · AlphaFold monomer V2.0 prediction for D-allose-binding periplasmic protein (P39265) · a predicted model of the same protein · chain B against A, TM-score 0.85
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 P39265
- Elsewhere: RCSB PDB 1GUD · PDBe 1GUD · UniProt P39265
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