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The crystal structure analysis of creatine amidinohydrolase from actinobacillus
Analyse The crystal structure analysis of creatine amidinohydrolase from actinobacillus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KP0
- Type
- protein
- Length
- 804 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Creatine amidinohydrolase
- EC
- 3.5.3.3
- UniProt
- Q7SIB5
- Pockets
- 2 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Creatine amidinohydrolase (EC 3.5.3.3) | protein | 402 | 37% helix, 25% strand | Q7SIB5 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 450 | 0.87 | 0.94 | 58 | empty |
| 2 | 1069 | 0.85 | 0.86 | 98 | empty |
Interfaces
1 interface between chains.
- A–B · 3659 Ų buried · 40 hydrogen bonds · protein-protein
Compared structures
- 1KP0 · The Crystal Structure Analysis of Creatine Amidinohydrolase from Actinobacillus · 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 Q7SIB5
- Elsewhere: RCSB PDB 1KP0 · PDBe 1KP0 · UniProt Q7SIB5
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