Research workbench
Crystal structure of the ancestral soluble variant of the human phosphate binding protein (hpbp)
Analyse Crystal structure of the ancestral soluble variant of the human phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4M1V
- Type
- protein
- Length
- 378 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphate-binding protein
- UniProt
- P85173
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphate-binding protein | protein | 378 | 33% helix, 19% strand | P85173 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 6 copies · chains A
- ACT · Acetate ion · additive · chains A
- GOL · Glycerol · additive · chains A
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 | 83 | 0.33 | 0.74 | 21 | EDO |
| 2 | 60 | 0.29 | 0.74 | 19 | EDO, GOL |
| 3 | 53 | 0.29 | 0.75 | 18 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4M1V · Crystal structure of the ancestral soluble variant of the Human Phosphate Binding Protein… · the same entry in another collection · chain A against A, TM-score 1.00
- P85173 · AlphaFold monomer V2.0 prediction for phosphate-binding protein (P85173) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P85173
- Elsewhere: RCSB PDB 4M1V · PDBe 4M1V · UniProt P85173
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