Research workbench
Crystal and cryoem structural studies of a cell wall degrading enzyme in the bacteriophage PHI29 tail
Analyse Crystal and cryoem structural studies of a cell wall degrading enzyme in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CSQ
- Type
- protein
- Length
- 1,298 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Morphogenesis protein 1
- UniProt
- P15132
- Ligands
- ZN
- Pockets
- 9 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Morphogenesis protein 1 | protein | 324 | 28% helix, 21% strand | P15132 |
| D | Morphogenesis protein 1 | protein | 326 | 28% helix, 20% strand | P15132 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1098 | 0.77 | 0.79 | 101 | empty |
| 2 | 586 | 0.75 | 0.82 | 67 | empty |
| 3 | 566 | 0.68 | 0.78 | 37 | empty |
| 4 | 253 | 0.63 | 0.81 | 37 | empty |
| 5 | 102 | 0.59 | 0.86 | 19 | empty |
Interfaces
4 interfaces between chains.
- B–D · 1049 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 724 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 648 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 26 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3CSQ · Crystal and cryoEM structural studies of a cell wall degrading enzyme in the… · 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 P15132
- Elsewhere: RCSB PDB 3CSQ · PDBe 3CSQ · UniProt P15132
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