MolNFT v1 · #31183 · protein
Crystal structure of LMO0035 protein (46906266) from listeria monocytogenes 4B F2365 at 1.50 a resolution
2AML · Sis domain protein: “Crystal structure of LMO0035 protein (46906266) from listeria monocytogenes 4B F2365 at 1.50 a resolution”. X-ray diffraction, 1 ligand (PO4), 4 pockets (best druggability 0.86). MolNFT v1 #31183 on GenesisL1…
- PDB
- 2AML
- Type
- protein
- Length
- 727 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sis domain protein
- UniProt
- Q4EK90
- Ligands
- PO4
- Pockets
- 4 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sis domain protein | protein | 366 | 49% helix, 14% strand | Q4EK90 |
| B | Sis domain protein | protein | 361 | 50% helix, 15% strand | Q4EK90 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains A, B
- ACT · Acetate ion · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1150 | 0.86 | 0.87 | 89 | empty |
| 2 | 344 | 0.81 | 0.91 | 57 | PO4 |
| 3 | 332 | 0.80 | 0.91 | 56 | ACT, PO4 |
| 4 | 58 | 0.30 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 3128 Ų buried · 31 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 2AML · Crystal structure of Lmo0035 protein (46906266) from LISTERIA MONOCYTOGENES 4b F2365 at… · 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 Q4EK90
- Elsewhere: RCSB PDB 2AML · PDBe 2AML · UniProt Q4EK90
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