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Crystal structure of probable P-nitrophenyl phosphatase (PHO2) (target efi-501307) from archaeoglobus fulgidus dsm 4304 with magnesium bound
Analyse Crystal structure of probable P-nitrophenyl phosphatase (PHO2) (target… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4JDP
- Type
- protein
- Length
- 529 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- P-nitrophenyl phosphatase (PHO2)
- UniProt
- O29873
- Ligands
- MG, CL
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | P-nitrophenyl phosphatase (PHO2) | protein | 264 | 41% helix, 21% strand | O29873 |
| B | P-nitrophenyl phosphatase (PHO2) | protein | 265 | 41% helix, 19% strand | O29873 |
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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 312 | 0.70 | 0.84 | 36 | CL |
| 2 | 425 | 0.70 | 0.81 | 49 | MG, CL |
| 3 | 116 | 0.41 | 0.76 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1298 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 4JDP · Crystal structure of probable p-nitrophenyl phosphatase (pho2) (target EFI-501307) from… · 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 O29873
- Elsewhere: RCSB PDB 4JDP · PDBe 4JDP · UniProt O29873
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