Research workbench
The crystal structure of the protein LIN1944 from listeria innocua .
Analyse The crystal structure of the protein LIN1944 from listeria innocua . in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3D7L
- Type
- protein
- Length
- 1,804 residues
- Chains
- 9
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- LIN1944 protein
- UniProt
- Q92AH8
- Pockets
- 20 · best druggability 0.76
Structure
x-ray diffraction · 4 distinct chains · 47% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, H | LIN1944 protein | protein | 202 | 45% helix, 21% strand | Q92AH8 |
| B, C, E, G, I | LIN1944 protein | protein | 200 | 47% helix, 21% strand | Q92AH8 |
| D | LIN1944 protein | protein | 201 | 47% helix, 21% strand | Q92AH8 |
| F | LIN1944 protein | protein | 199 | 48% helix, 21% strand | Q92AH8 |
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 953 | 0.76 | 0.79 | 61 | empty |
| 2 | 947 | 0.74 | 0.77 | 88 | empty |
| 3 | 881 | 0.74 | 0.78 | 97 | empty |
| 4 | 672 | 0.73 | 0.80 | 79 | empty |
| 5 | 778 | 0.73 | 0.78 | 85 | empty |
Interfaces
19 interfaces between chains.
- C–D · 1518 Ų buried · 5 hydrogen bonds · protein-protein
- G–H · 1518 Ų buried · 7 hydrogen bonds · protein-protein
- E–F · 1508 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 1505 Ų buried · 6 hydrogen bonds · protein-protein
- A–H · 519 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 54 modified (engineered).
Compared structures
- 3D7L · The crystal structure of the protein lin1944 from Listeria innocua . · 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 Q92AH8
- Elsewhere: RCSB PDB 3D7L · PDBe 3D7L · UniProt Q92AH8
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