MolNFT v1 · #26864 · protein
Crystal structure of lipate-protein ligase a from escherichia COLI
1X2G · Lipoate-protein ligase a: “Crystal structure of lipate-protein ligase a from escherichia COLI”. X-ray diffraction, 13 pockets (best druggability 0.83). MolNFT v1 #26864 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1X2G
- Type
- protein
- Length
- 998 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipoate-protein ligase a
- EC
- 6.3.2.-
- UniProt
- P32099
- Pockets
- 13 · best druggability 0.83
Structure
x-ray diffraction · 3 distinct chains · 35% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipoate-protein ligase a (EC 6.3.2.-) | protein | 331 | 36% helix, 28% strand | P32099 |
| B | Lipoate-protein ligase a (EC 6.3.2.-) | protein | 330 | 36% helix, 28% strand | P32099 |
| C | Lipoate-protein ligase a (EC 6.3.2.-) | protein | 337 | 34% helix, 27% strand | P32099 |
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 384 | 0.83 | 0.91 | 49 | empty |
| 2 | 169 | 0.73 | 0.91 | 36 | empty |
| 3 | 205 | 0.73 | 0.89 | 41 | empty |
| 4 | 478 | 0.71 | 0.81 | 48 | empty |
| 5 | 429 | 0.70 | 0.81 | 46 | empty |
Interfaces
3 interfaces between chains.
- A–C · 2272 Ų buried · 37 hydrogen bonds · protein-protein
- A–B · 1151 Ų buried · 23 hydrogen bonds · protein-protein
- B–C · 207 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 15 modified (engineered).
Compared structures
- 1X2G · Crystal Structure of Lipate-Protein Ligase A from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
- P32099 · AlphaFold monomer V2.0 prediction for lipoate-protein ligase a (P32099) · a predicted model of the same protein · chain A against A, TM-score 0.87
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 P32099
- Elsewhere: RCSB PDB 1X2G · PDBe 1X2G · UniProt P32099
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