MolNFT v1 · #92975 · protein
Crystal structure of a putative methionine-binding lipoprotein (BSU32730) from bacillus subtilis subsp. subtilis str. 168 at 1.95 a resolution
4GOT · Methionine-binding lipoprotein metq: “Crystal structure of a putative methionine-binding lipoprotein (BSU32730) from bacillus subtilis subsp.…”. X-ray diffraction, 2 ligands (MSE, SO4), 1 pocket (best druggability 0.38). MolNFT v1…
- PDB
- 4GOT
- Type
- protein
- Length
- 247 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methionine-binding lipoprotein metq
- UniProt
- O32167
- Ligands
- MSE, SO4
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine-binding lipoprotein metq | protein | 247 | 37% helix, 23% strand | O32167 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 91 | 0.38 | 0.76 | 16 | empty |
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 4GOT · Crystal structure of a putative methionine-binding lipoprotein (BSU32730) from Bacillus… · the same entry in another collection · chain A against A, TM-score 1.00
- O32167 · AlphaFold monomer V2.0 prediction for methionine-binding lipoprotein metq (O32167) · a predicted model of the same protein · 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 O32167
- Elsewhere: RCSB PDB 4GOT · PDBe 4GOT · UniProt O32167
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