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Low temperature structure of P22 tailspike protein fragment (109-666), mutant V349L

Analyse Low temperature structure of P22 tailspike protein fragment (109-666), mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2VFP
Type: protein
Length: 556 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: P22 tailspike protein
EC: 3.2.1.-
UniProt: P12528
Ligands: CA, SO4
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	P22 tailspike protein (EC 3.2.1.-)	protein	556	8% helix, 41% strand	P12528

Ligands and binding sites

CA · Calcium ion · metal · chains A
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · 6 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	489	0.64	0.76	53	GOL
2	52	0.29	0.76	13	empty

Compared structures

2VFP · Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V349L · 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 2VFP · PDBe 2VFP · UniProt P12528

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