2GOM: Efb-C from Staphylococcus aureus

Crystal structure of Efb-C from Staphylococcus aureus. Determined by X-ray diffraction at 1.25 Å resolution. Released 20 Mar 2007.

Method: X-ray diffraction
Resolution: 1.25 Å
Organism: Staphylococcus aureus
Chains: 2
Atoms: 1,142
Mol. weight: 14.41 kDa
Released: 20 Mar 2007

Explore 2GOM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2GOM contains 7 α-helices and 4 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	106-124	19
β-strand	126	1	1
α-helix	127-139	13
α-helix	142-144	3
α-helix	145-161	17
β-strand	164	1	1

Chain B: 3 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	107-124	18
β-strand	126	1	2
α-helix	127-139	13
α-helix	145-161	17
β-strand	164	1	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fibrinogen-binding protein	A, B	protein	61	Staphylococcus aureus	P68799 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2GOM_1 Fibrinogen-binding protein (chains A, B)
IKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYKVKKMVLQERIDNVLKQGLV
R

Primary citation

A structural basis for complement inhibition by Staphylococcus aureus. Hammel, M., Sfyroera, G., Ricklin, D. et al. Nat Immunol (2007) 8:430-437. DOI 10.1038/ni1450 · PubMed

Other PDB entries of the same protein (UniProt P68799 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2GOX 2.2 Å, Crystal structure of Efb-C / C3d Complex
9N20 3.3 Å, Structure of C3d Bound to a Fragment of FHR-2 and S. aureus Efb-C

Browse structure collections

About this viewer

MolViewer shows 2GOM directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.