3ZD1: Complement factor H-related protein 2

Structure of the two C-terminal domains of complement factor H related protein 2. Determined by X-ray diffraction at 2.0 Å resolution. Released 13 Mar 2013.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 2,069
Mol. weight: 29.23 kDa
Released: 13 Mar 2013

Explore 3ZD1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3ZD1 contains 12 α-helices and 41 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: 6 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	131	1	1
α-helix	134-136	3
β-strand	140-142	3	2
β-strand	150	1	1
β-strand	155-157	3	3
β-strand	158-160	3	2
α-helix	161	1
β-strand	165-167	3	4
β-strand	171-173	3	3
β-strand	174-175	2	5
β-strand	178-179	2	5
α-helix	180-182	3
β-strand	184-186	3	4
α-helix	187-188	2
β-strand	189-190	2	6
α-helix	193-198	6
β-strand	201-203	3	7
β-strand	212-213	2	6
β-strand	218-220	3	8
β-strand	221-223	3	7
α-helix	224	1
β-strand	228-229	2	9
β-strand	236-238	3	8
β-strand	240	1	10
β-strand	243	1	10
β-strand	249-250	2	9

Chain B: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	131	1	11
α-helix	134-136	3
β-strand	137	1	12
β-strand	140-142	3	12
β-strand	150	1	11
β-strand	155-157	3	13
β-strand	158-160	3	12
β-strand	165-167	3	14
β-strand	171-173	3	13
β-strand	174-175	2	15
β-strand	178-179	2	15
β-strand	184-186	3	14
α-helix	187-188	2
β-strand	189-190	2	16
α-helix	191	1
α-helix	193-198	6
β-strand	201-203	3	17
β-strand	212-213	2	16
β-strand	218-220	3	18
β-strand	221-223	3	17
α-helix	224	1
β-strand	228-229	2	19
β-strand	236-238	3	18
α-helix	239	1
β-strand	240	1	20
β-strand	243	1	20
β-strand	249-250	2	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement factor H-related protein 2	A, B	protein	126	HOMO SAPIENS	P36980 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3ZD1_1 COMPLEMENT FACTOR H-RELATED PROTEIN 2 (chains A, B)
MGEKCGPPPPIDNGDITSFLLSVYAPGSSVEYQCQNLYQLEGNNQITCRNGQWSEPPKCL
DPCVISQEIMEKYNIKLKWTNQQKLYSRTGDIVEFVCKSGYHPTKSHSFRAMCQNGKLVY
PSCEEK

Primary citation

Dimerization of Complement Factor H-Related Proteins Modulates Complement Activation in Vivo. Goicoechea De Jorge, E., Caesar, J.J.E., Malik, T.H. et al. Proc Natl Acad Sci U S A (2013) 110:4685. DOI 10.1073/PNAS.1219260110 · PubMed

Other PDB entries of the same protein (UniProt P36980 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5EA0 2.0 Å, Structure of the antibody 7968 with human complement factor H-derived peptide
9N1Z 2.31 Å, Structure of C3d Bound to a Fragment of FHR-2
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 3ZD1 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.