Research workbench
Hrsv M2-1, P422 crystal form
Analyse Hrsv M2-1, P422 crystal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C3D
- Type
- protein
- Length
- 321 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Matrix M2-1
- UniProt
- P04545
- Ligands
- CD
- Pockets
- 2 · best druggability 0.31
Structure
x-ray diffraction · 2 distinct chains · 68% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Matrix M2-1 | protein | 165 | 65% helix, 1% strand | P04545 |
| B | Matrix M2-1 | protein | 156 | 71% helix, 1% strand | P04545 |
Ligands and binding sites
- CD · Cadmium ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 55 | 0.31 | 0.76 | 12 | empty |
| 2 | 61 | 0.29 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 323 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 4C3D · HRSV M2-1, P422 crystal form · 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 P04545
- Elsewhere: RCSB PDB 4C3D · PDBe 4C3D · UniProt P04545
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