MolNFT v1 · #70593 · protein
P15 HIV rnaseh domain with inhibitor MK3
3LP3: “P15 HIV rnaseh domain with inhibitor MK3”. X-ray diffraction, 2 ligands (LP9, MN). MolNFT v1 #70593 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3LP3
- Type
- protein
- Length
- 262 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- P15
- UniProt
- P0C6F2
- Ligands
- LP9, MN
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | P15 | protein | 131 | 34% helix, 27% strand | P0C6F2 |
Ligands and binding sites
- LP9 · 3-[4-(diethylamino)phenoxy]-6-(ethoxycarbonyl)-5,8-dihydroxy-7-oxo-7,8-dihydro-1,8-naphthyridin-1-ium · ligand · 2 copies · chains A, B
- MN · Manganese (II) ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 458 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 3LP3 · p15 HIV RNaseH domain with inhibitor MK3 · 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 P0C6F2
- Elsewhere: RCSB PDB 3LP3 · PDBe 3LP3 · UniProt P0C6F2
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