MolNFT v1 · #99359 · protein

Crystal structure of the N-terminal fic domain of bartonella effector protein (bep); substrate of virb T4SS (virb-translocated bep effector protein) from bartonella sp. ar 15-3

4M16 · Bartonella effector protein (bep) substrate of virb T4SS: “Crystal structure of the N-terminal fic domain of bartonella effector protein (bep); substrate of virb T4SS…”. X-ray diffraction, 2 pockets (best druggability 0.66). MolNFT…

PDB: 4M16
Type: protein
Length: 225 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bartonella effector protein (bep) substrate of virb T4SS
UniProt: E6YQQ1
Pockets: 2 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bartonella effector protein (bep) substrate of virb T4SS	protein	225	55% helix, 4% strand	E6YQQ1

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	619	0.66	0.76	55	EDO
2	61	0.29	0.74	11	empty

Compared structures

4M16 · Crystal Structure of the N-terminal Fic Domain of Bartonella effector protein (Bep)… · 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 E6YQQ1
Elsewhere: RCSB PDB 4M16 · PDBe 4M16 · UniProt E6YQQ1

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