MolNFT v1 · #51713 · protein
Low temperature structure of P22 tailspike protein fragment (109-666), mutant V125A
2VFN · Bifunctional tail protein: “Low temperature structure of P22 tailspike protein fragment (109-666), mutant V125A”. X-ray diffraction, 2 ligands (CA, SO4), 2 pockets (best druggability 0.63). MolNFT v1 #51713 on GenesisL1: 3D…
- PDB
- 2VFN
- Type
- protein
- Length
- 555 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional tail protein
- EC
- 3.2.1.-
- UniProt
- P12528
- Ligands
- CA, SO4
- Pockets
- 2 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional tail protein (EC 3.2.1.-) | protein | 555 | 8% helix, 42% strand | P12528 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · 10 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 463 | 0.63 | 0.76 | 52 | GOL |
| 2 | 59 | 0.40 | 0.81 | 19 | empty |
Compared structures
- 2VFN · Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V125A · 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 P12528
- Elsewhere: RCSB PDB 2VFN · PDBe 2VFN · UniProt P12528
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