Research workbench
Caulobacter bacteriophage 5
Analyse Caulobacter bacteriophage 5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2W4Z
- Type
- protein
- Length
- 366 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caulobacter bacteriophage 5
- Ligands
- AMP, CA
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Caulobacter bacteriophage 5 | protein | 122 | 18% helix, 48% strand | — |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · 3 copies · chains A, B, C
- CA · Calcium ion · metal · 4 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 939 | 0.76 | 0.79 | 106 | AMP |
| 2 | 72 | 0.33 | 0.75 | 12 | empty |
| 3 | 52 | 0.28 | 0.74 | 13 | empty |
Interfaces
3 interfaces between chains.
- A–B · 410 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 409 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 306 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 2W4Z · Caulobacter bacteriophage 5 · 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
- Elsewhere: RCSB PDB 2W4Z · PDBe 2W4Z
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