Research workbench
Structural genomics, the crystal structure of a putative ABC transporter domain from porphyromonas gingivalis W83
Analyse Structural genomics, the crystal structure of a putative ABC transporter domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2P0S
- Type
- protein
- Length
- 252 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ABC transporter, permease protein, putative
- UniProt
- Q7MVU4
- Ligands
- MG
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ABC transporter, permease protein, putative | protein | 130 | 35% helix, 18% strand | Q7MVU4 |
| B | ABC transporter, permease protein, putative | protein | 122 | 35% helix, 21% strand | Q7MVU4 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
- FMT · Formic acid · 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
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 | 447 | 0.64 | 0.78 | 62 | empty |
| 2 | 79 | 0.33 | 0.74 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 2550 Ų buried · 30 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 2P0S · Structural Genomics, the crystal structure of a putative ABC transporter domain from… · 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 Q7MVU4
- Elsewhere: RCSB PDB 2P0S · PDBe 2P0S · UniProt Q7MVU4
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