Research workbench

Structure of a mutant of ospa

Analyse Structure of a mutant of ospa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7FJR
Type: protein
Length: 240 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Outer surface protein a
UniProt: P0CL66
Pockets: 2 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Outer surface protein a	protein	240	3% helix, 52% strand	P0CL66

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · 2 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	103	0.41	0.77	22	empty
2	78	0.31	0.73	16	PEG

Compared structures

7FJR · Structure of a mutant of OspA · the same entry in another collection · chain A against A, TM-score 1.00
P0CL66 · AlphaFold monomer V2.0 prediction for outer surface protein a (P0CL66) · a predicted model of the same protein · chain A against A, TM-score 0.59

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 P0CL66
Elsewhere: RCSB PDB 7FJR · PDBe 7FJR · UniProt P0CL66

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