Research workbench
Phosphate-binding protein mutant with asp 137 replaced by thr complex with chlorine and phosphate
Analyse Phosphate-binding protein mutant with asp 137 replaced by thr complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QUL
- Type
- protein
- Length
- 321 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphate-binding protein
- UniProt
- P06128
- Ligands
- PO4, CL
- Pockets
- 3 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphate-binding protein | protein | 321 | 39% helix, 22% strand | P06128 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.41 | 0.81 | 12 | empty |
| 2 | 57 | 0.38 | 0.80 | 17 | empty |
| 3 | 57 | 0.27 | 0.74 | 17 | empty |
Compared structures
- 1QUL · Phosphate-binding protein mutant with asp 137 replaced by thr complex with chlorine and… · 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 P06128
- Elsewhere: RCSB PDB 1QUL · PDBe 1QUL · UniProt P06128
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