Research workbench
Crystal structure of an atmb (putative membrane lipoprotein) from streptococcus mutans UA159 at 1.91 a resolution
Analyse Crystal structure of an atmb (putative membrane lipoprotein) from streptococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Q5T
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipoprotein
- UniProt
- I6L927
- Ligands
- MSE
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipoprotein | protein | 257 | 39% helix, 26% strand | I6L927 |
Ligands and binding sites
- MSE · Selenomethionine · ligand · chains A
- 2PE · Nonaethylene glycol · additive · 3 copies · chains A
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 | 142 | 0.74 | 0.92 | 35 | MSE |
| 2 | 95 | 0.41 | 0.78 | 22 | empty |
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 4Q5T · Crystal structure of an atmB (putative membrane lipoprotein) from Streptococcus mutans… · 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 I6L927
- Elsewhere: RCSB PDB 4Q5T · PDBe 4Q5T · UniProt I6L927
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