Research workbench
X-ray structure of autolysin ACD24020 catalytic domain from clostridium difficile
Analyse X-ray structure of autolysin ACD24020 catalytic domain from clostridium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CFL
- Type
- protein
- Length
- 493 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative cell wall hydrolase phosphatase-associated protein
- EC
- 3.4.-.-
- UniProt
- Q181Y8
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative cell wall hydrolase phosphatase-associated protein (EC 3.4.-.-) | protein | 127 | 27% helix, 28% strand | Q181Y8 |
| B, C, D | Putative cell wall hydrolase phosphatase-associated protein (EC 3.4.-.-) | protein | 122 | 29% helix, 30% strand | Q181Y8 |
Ligands and binding sites
- FLC · Citrate anion · additive · 4 copies · chains A, B, C, D
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 | 658 | 0.67 | 0.76 | 64 | FLC |
| 2 | 423 | 0.64 | 0.78 | 49 | FLC |
| 3 | 110 | 0.45 | 0.78 | 19 | empty |
Interfaces
4 interfaces between chains.
- A–B · 501 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 328 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 322 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 287 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 7CFL · X-ray structure of autolysin Acd24020 catalytic domain 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 Q181Y8
- Elsewhere: RCSB PDB 7CFL · PDBe 7CFL · UniProt Q181Y8
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