Research workbench
Crystal structure of the periplasmic lysine-, arginine-, ornithine- binding protein (lao) S72A mutant from salmonella typhimurium complexed with arginine
Analyse Crystal structure of the periplasmic lysine-, arginine-, ornithine- binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MLN
- Type
- protein
- Length
- 235 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- LYSINE/ARGININE/ORNITHINE-binding periplasmic protein
- UniProt
- P02911
- Ligands
- ARG
- Pockets
- 1 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | LYSINE/ARGININE/ORNITHINE-binding periplasmic protein | protein | 235 | 36% helix, 23% strand | P02911 |
Ligands and binding sites
- ARG · Arginine · ligand · chains E
- GOL · Glycerol · additive · 5 copies · chains E
- ACT · Acetate ion · additive · 2 copies · chains E
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 | 86 | 0.35 | 0.75 | 17 | GOL |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6MLN · Crystal structure of the periplasmic Lysine-, Arginine-, Ornithine-binding protein (LAO)… · the same entry in another collection · chain E against E, TM-score 1.00
- P02911 · AlphaFold monomer V2.0 prediction for LYSINE/ARGININE/ORNITHINE- binding periplasmic… · a predicted model of the same protein · chain E 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 P02911
- Elsewhere: RCSB PDB 6MLN · PDBe 6MLN · UniProt P02911
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