Research workbench
Crystal structure of an empty substrate binding domain 1 (SBD1) of ABC transporter glnpq from lactococcus lactis
Analyse Crystal structure of an empty substrate binding domain 1 (SBD1) of ABC… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LA9
- Type
- protein
- Length
- 451 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamine ABC transporter permease and substrate binding protein protein
- UniProt
- Q9CES5
- Ligands
- PO4
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamine ABC transporter permease and substrate binding protein protein | protein | 226 | 38% helix, 23% strand | Q9CES5 |
| B | Glutamine ABC transporter permease and substrate binding protein protein | protein | 225 | 38% helix, 24% strand | Q9CES5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1052 | 0.81 | 0.82 | 83 | empty |
| 2 | 233 | 0.49 | 0.74 | 36 | PEG |
| 3 | 203 | 0.46 | 0.74 | 36 | PO4 |
| 4 | 117 | 0.36 | 0.73 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 551 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 4LA9 · Crystal structure of an empty substrate binding domain 1 (SBD1) OF ABC TRANSPORTER GLNPQ… · 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 Q9CES5
- Elsewhere: RCSB PDB 4LA9 · PDBe 4LA9 · UniProt Q9CES5
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