Research workbench
Crystal structure of putative peptidase from chlamydophila abortus
Analyse Crystal structure of putative peptidase from chlamydophila abortus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CE2
- Type
- protein
- Length
- 595 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative peptidase
- UniProt
- Q5L5N2
- Ligands
- ZN
- Pockets
- 5 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 66% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative peptidase | protein | 595 | 66% helix, 3% strand | Q5L5N2 |
Ligands and binding sites
- ZN · Zinc ion · metal · 6 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 659 | 0.72 | 0.79 | 73 | empty |
| 2 | 54 | 0.57 | 0.90 | 14 | empty |
| 3 | 300 | 0.55 | 0.75 | 42 | empty |
| 4 | 244 | 0.50 | 0.74 | 36 | empty |
| 5 | 117 | 0.37 | 0.73 | 22 | empty |
Compared structures
- 3CE2 · Crystal structure of putative peptidase from Chlamydophila abortus · 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 Q5L5N2
- Elsewhere: RCSB PDB 3CE2 · PDBe 3CE2 · UniProt Q5L5N2
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