Research workbench
Structure of recombinant haemophilus influenzae E(P4) acid phosphatase mutant D64N complexed with 5'AMP
Analyse Structure of recombinant haemophilus influenzae E(P4) acid phosphatase mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SF0
- Type
- protein
- Length
- 247 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipoprotein E
- EC
- 3.1.3.2
- UniProt
- P26093
- Ligands
- AMP, MG
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipoprotein E (EC 3.1.3.2) | protein | 247 | 51% helix, 15% strand | P26093 |
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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 404 | 0.69 | 0.81 | 49 | MG, AMP |
| 2 | 63 | 0.34 | 0.77 | 15 | empty |
| 3 | 88 | 0.32 | 0.73 | 18 | empty |
Compared structures
- 3SF0 · Structure of Recombinant Haemophilus Influenzae e(P4) Acid Phosphatase mutant D64N… · the same entry in another collection · chain A against A, TM-score 1.00
- P26093 · AlphaFold monomer V2.0 prediction for lipoprotein E (P26093) · 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 P26093
- Elsewhere: RCSB PDB 3SF0 · PDBe 3SF0 · UniProt P26093
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