Research workbench
Crystal structure of a putative peptide binding protein appa from clostridium difficile
Analyse Crystal structure of a putative peptide binding protein appa from clostridium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6I3G
- Type
- protein
- Length
- 479 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ABC transporter, substrate-binding protein, family 5
- UniProt
- A0A069AL86
- Ligands
- IOD, SO4
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ABC transporter, substrate-binding protein, family 5 | protein | 479 | 34% helix, 26% strand | A0A069AL86 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 972 | 0.76 | 0.78 | 85 | empty |
| 2 | 178 | 0.56 | 0.80 | 26 | empty |
| 3 | 55 | 0.34 | 0.78 | 17 | empty |
Compared structures
- 6I3G · Crystal structure of a putative peptide binding protein AppA from Clostridium difficile · 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 A0A069AL86
- Elsewhere: RCSB PDB 6I3G · PDBe 6I3G · UniProt A0A069AL86
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