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Structure of complement regulator-acquiring surface protein 3 (crasp- 3, erpp or BBN38) from borrelia burgdorferi

Analyse Structure of complement regulator-acquiring surface protein 3 (crasp- 3, erpp… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4BOB
Type: protein
Length: 132 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Erpp protein
UniProt: Q9S036
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Erpp protein	protein	132	17% helix, 52% strand	Q9S036

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	71	0.36	0.77	16	empty

Compared structures

4BOB · Structure of Complement regulator-acquiring surface protein 3 (CRASP- 3, ErpP or BBN38)… · 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 Q9S036
Elsewhere: RCSB PDB 4BOB · PDBe 4BOB · UniProt Q9S036

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