Research workbench
Structure of an E. COLI exopolyphosphatase: insight into the processive hydrolysis of polyphosphate and its regulation
Analyse Structure of an E. COLI exopolyphosphatase: insight into the processive… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1U6Z
- Type
- protein
- Length
- 998 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Exopolyphosphatase
- EC
- 3.6.1.11
- UniProt
- P29014
- Ligands
- SO4
- Pockets
- 13 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Exopolyphosphatase (EC 3.6.1.11) | protein | 498 | 50% helix, 17% strand | P29014 |
| B | Exopolyphosphatase (EC 3.6.1.11) | protein | 500 | 51% helix, 17% strand | P29014 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 29 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1044 | 0.79 | 0.81 | 79 | SO4 |
| 2 | 1114 | 0.77 | 0.80 | 104 | SO4 |
| 3 | 180 | 0.71 | 0.89 | 35 | SO4 |
| 4 | 352 | 0.70 | 0.83 | 53 | SO4 |
| 5 | 336 | 0.62 | 0.78 | 41 | SO4 |
Interfaces
1 interface between chains.
- A–B · 1569 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 1U6Z · Structure of an E. coli Exopolyphosphatase: Insight into the processive hydrolysis of… · 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 P29014
- Elsewhere: RCSB PDB 1U6Z · PDBe 1U6Z · UniProt P29014
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