MolNFT v1 · #64382 · protein
Crystals structure of phnp from E.COLI K-12
3G1P · Protein phnp: “Crystals structure of phnp from E.COLI K-12”. X-ray diffraction, 3 ligands (MLT, MN, ZN), 2 pockets (best druggability 0.71). MolNFT v1 #64382 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3G1P
- Type
- protein
- Length
- 499 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein phnp
- UniProt
- P16692
- Ligands
- MLT, MN, ZN
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein phnp | protein | 249 | 20% helix, 30% strand | P16692 |
| B | Protein phnp | protein | 250 | 20% helix, 31% strand | P16692 |
Ligands and binding sites
- MLT · D-malate · ligand · 2 copies · chains A, B
- MN · Manganese (II) ion · metal · 4 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 515 | 0.71 | 0.80 | 56 | MLT |
| 2 | 438 | 0.68 | 0.80 | 48 | MLT |
Interfaces
1 interface between chains.
- A–B · 1155 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
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 P16692
- Elsewhere: RCSB PDB 3G1P · PDBe 3G1P · UniProt P16692
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