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Low temperature structure of P22 tailspike protein fragment (109-666), mutant V125L

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: 2VFO
Type: protein
Length: 555 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: P22 tailspike protein, mutant V125L
EC: 3.2.1.-
UniProt: P12528
Ligands: CA, SO4
Pockets: 3 · best druggability 0.62

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	P22 tailspike protein, mutant V125L (EC 3.2.1.-)	protein	555	8% helix, 41% strand	P12528

Ligands and binding sites

CA · Calcium ion · metal · chains A
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · 7 copies · chains A

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	401	0.62	0.77	33	GOL
2	120	0.39	0.75	23	GOL
3	52	0.25	0.72	8	empty

Compared structures

2VFO · Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V125L · 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 2VFO · PDBe 2VFO · UniProt P12528

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