MolNFT v1 · #7391 · protein
Bacteriophage lambda SER/THR protein phosphatase
1G5B · SERINE/THREONINE protein phosphatase: “Bacteriophage lambda SER/THR protein phosphatase”. X-ray diffraction, 3 ligands (MN, HG, SO4), 6 pockets (best druggability 0.65). MolNFT v1 #7391 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1G5B
- Type
- protein
- Length
- 661 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE protein phosphatase
- EC
- 3.1.3.-
- UniProt
- P03772
- Ligands
- MN, HG, SO4
- Pockets
- 6 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE protein phosphatase (EC 3.1.3.-) | protein | 219 | 34% helix, 20% strand | P03772 |
| B, C | SERINE/THREONINE protein phosphatase (EC 3.1.3.-) | protein | 221 | 34% helix, 19% strand | P03772 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 6 copies · chains A, B, C
- HG · Mercury (II) ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 408 | 0.65 | 0.79 | 39 | MN, HG, SO4 |
| 2 | 165 | 0.49 | 0.77 | 24 | empty |
| 3 | 57 | 0.33 | 0.77 | 11 | empty |
| 4 | 66 | 0.30 | 0.74 | 18 | MN, SO4 |
| 5 | 56 | 0.29 | 0.75 | 12 | empty |
Interfaces
2 interfaces between chains.
- A–C · 511 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 338 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1G5B · Bacteriophage lambda SER/THR protein phosphatase · 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 P03772
- Elsewhere: RCSB PDB 1G5B · PDBe 1G5B · UniProt P03772
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