Research workbench
Crystal structure of bacillus anthracis transpeptidase enzyme capd, crystal form II
Analyse Crystal structure of bacillus anthracis transpeptidase enzyme capd, crystal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GA9
- Type
- protein
- Length
- 455 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsule biosynthesis protein capd
- UniProt
- Q51693
- Pockets
- 6 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | Capsule biosynthesis protein capd | protein | 286 | 53% helix, 13% strand | Q51693 |
| S | Capsule biosynthesis protein capd | protein | 169 | 22% helix, 31% strand | Q51693 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 70 | 0.56 | 0.88 | 18 | empty |
| 2 | 83 | 0.48 | 0.83 | 18 | empty |
| 3 | 86 | 0.42 | 0.78 | 15 | empty |
| 4 | 107 | 0.40 | 0.76 | 17 | empty |
| 5 | 93 | 0.39 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- L–S · 4748 Ų buried · 88 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 13 modified (engineered).
Compared structures
- 3GA9 · Crystal structure of Bacillus anthracis transpeptidase enzyme CapD, crystal form II · the same entry in another collection · chain L against L, TM-score 1.00
- Q51693 · AlphaFold monomer V2.0 prediction for capsule biosynthesis protein capd proenzyme (Q51693) · a predicted model of the same protein · chain L against A, TM-score 0.98
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 Q51693
- Elsewhere: RCSB PDB 3GA9 · PDBe 3GA9 · UniProt Q51693
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