MolNFT v1 · #86720 · protein

Erpc, a member of the complement regulator acquiring family of surface proteins from borrelia burgdorfei, possesses an architecture previously unseen in this protein family.

4BF3: “Erpc, a member of the complement regulator acquiring family of surface proteins from borrelia burgdorfei…”. X-ray diffraction, 1 pocket (best druggability 0.46). MolNFT v1 #86720 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 4BF3
Type: protein
Length: 261 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Erpc
UniProt: Q44790
Pockets: 1 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 16% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Erpc	protein	133	16% helix, 53% strand	Q44790
B	Erpc	protein	128	16% helix, 52% strand	Q44790

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 5 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	149	0.46	0.77	25	EDO

Interfaces

1 interface between chains.

A–B · 561 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

4BF3 · ErpC, a member of the complement regulator acquiring family of surface proteins from… · 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 Q44790
Elsewhere: RCSB PDB 4BF3 · PDBe 4BF3 · UniProt Q44790

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