MolNFT v1 · #13790 · protein
Structure of the obg GTP-binding protein
1LNZ · SPO0B-associated GTP-binding protein: “Structure of the obg GTP-binding protein”. X-ray diffraction, 2 ligands (G4P, MG), 6 pockets (best druggability 0.66). MolNFT v1 #13790 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1LNZ
- Type
- protein
- Length
- 662 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SPO0B-associated GTP-binding protein
- UniProt
- P20964
- Ligands
- G4P, MG
- Pockets
- 6 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SPO0B-associated GTP-binding protein | protein | 342 | 19% helix, 25% strand | P20964 |
| B | SPO0B-associated GTP-binding protein | protein | 320 | 20% helix, 29% strand | P20964 |
Ligands and binding sites
- G4P · Guanosine-5',3'-tetraphosphate · ligand · chains B
- MG · Magnesium ion · metal · 7 copies · chains A, B
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 | 648 | 0.66 | 0.75 | 74 | empty |
| 2 | 69 | 0.42 | 0.80 | 13 | empty |
| 3 | 89 | 0.39 | 0.77 | 21 | empty |
| 4 | 103 | 0.37 | 0.75 | 20 | empty |
| 5 | 83 | 0.34 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 426 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 modified (engineered).
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 P20964
- Elsewhere: RCSB PDB 1LNZ · PDBe 1LNZ · UniProt P20964
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