MolNFT v1 · #118175 · protein

Fic domain of BEP1 from bartonella rochalimae in complex with biaa

5EU0 · Bartonella effector protein (bep) substrate of virb T4SS: “Fic domain of BEP1 from bartonella rochalimae in complex with biaa”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.70). MolNFT v1 #118175 on GenesisL1…

PDB: 5EU0
Type: protein
Length: 268 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bartonella effector protein (bep) substrate of virb T4SS; Antitoxin 1
UniProt: E6YJU0, E6YLF5
Ligands: SO4
Pockets: 2 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 57% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bartonella effector protein (bep) substrate of virb T4SS	protein	213	53% helix, 7% strand	E6YJU0
B	Antitoxin 1	protein	55	71% helix, 0% strand	E6YLF5

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A, B

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	418	0.70	0.81	46	SO4
2	117	0.46	0.79	16	empty

Interfaces

1 interface between chains.

A–B · 1139 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

5EU0 · FIC domain of Bep1 from Bartonella rochalimae in complex with BiaA · 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 E6YJU0
Every structure of UniProt E6YLF5
Elsewhere: RCSB PDB 5EU0 · PDBe 5EU0 · UniProt E6YJU0 · UniProt E6YLF5

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