MolNFT v1 · #25421 · protein
Crystal structure of a putative lipoate-protein ligase a (SP_1160) from streptococcus pneumoniae TIGR4 at 1.99 a resolution
1VQZ · Lipoate-protein ligase, putative: “Crystal structure of a putative lipoate-protein ligase a (SP_1160) from streptococcus pneumoniae TIGR4 at…”. X-ray diffraction, 1 ligand (UNL), 2 pockets (best druggability 0.62). MolNFT v1 #25421…
- PDB
- 1VQZ
- Type
- protein
- Length
- 330 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipoate-protein ligase, putative
- UniProt
- Q97QP1
- Ligands
- UNL
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipoate-protein ligase, putative | protein | 330 | 32% helix, 28% strand | Q97QP1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 431 | 0.62 | 0.77 | 56 | EDO |
| 2 | 132 | 0.42 | 0.76 | 26 | EDO |
Modifications
Observed in the structure: 4 modified, 1 covalent (engineered, covalent ligand).
Compared structures
- 1VQZ · Crystal structure of a putative lipoate-protein ligase a (sp_1160) from streptococcus… · 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 Q97QP1
- Elsewhere: RCSB PDB 1VQZ · PDBe 1VQZ · UniProt Q97QP1
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