2G7I: Complement factor H

Structure of Human Complement Factor H Carboxyl Terminal Domains 19-20: a Basis for Atypical Hemolytic Uremic Syndrome. Determined by X-ray diffraction at 1.75 Å resolution. Released 23 May 2006.

Method: X-ray diffraction
Resolution: 1.75 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,153
Mol. weight: 14.3 kDa
Released: 23 May 2006

Explore 2G7I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2G7I contains 7 α-helices and 21 β-strands across 1 chain. 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: 7 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	1109	1	1
α-helix	1112-1114	3
β-strand	1115	1	2
β-strand	1118-1120	3	2
β-strand	1128	1	1
β-strand	1133-1135	3	3
β-strand	1136-1138	3	2
β-strand	1143-1145	3	4
β-strand	1149-1151	3	3
β-strand	1152-1153	2	5
β-strand	1156-1157	2	5
α-helix	1158-1160	3
β-strand	1162-1164	3	4
α-helix	1165-1166	2
β-strand	1167-1168	2	6
α-helix	1171-1177	7
β-strand	1179-1181	3	7
β-strand	1190-1191	2	6
β-strand	1196-1198	3	8
β-strand	1199-1201	3	7
α-helix	1202	1
β-strand	1206-1207	2	9
α-helix	1208	1
α-helix	1211-1213	3
β-strand	1215-1217	3	8
β-strand	1219	1	10
β-strand	1222	1	10
β-strand	1228-1229	2	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement factor H	A	protein	125	Homo sapiens	P08603 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2G7I_1 Complement factor H (chains A)
GKCGPPPPIDNGDITSFPLSVYAPASSVEYQCQNLYQLEGNKRITCRNGQWSEPPKCLHP
CVISREIMENYNIALRWTAKQKLYSRTGESVEFVCKRGYRLSSRSHTLRTTCWDGKLEYP
TCAKR

Primary citation

Structure of complement factor H carboxyl-terminus reveals molecular basis of atypical haemolytic uremic syndrome. Jokiranta, T.S., Jaakola, V.-P., Lehtinen, M.J. et al. EMBO J (2006) 25:1784-1794. DOI 10.1038/sj.emboj.7601052 · PubMed

Other PDB entries of the same protein (UniProt P08603 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4K12 1.08 Å, Structural Basis for Host Specificity of Factor H Binding by Streptococcus pneumoniae
3R62 1.52 Å, Structure of complement regulator Factor H mutant, T1184R.
3KZJ 1.65 Å, Structure of complement Factor H variant R1203A
3SW0 1.8 Å, Structure of the C-terminal region (modules 18-20) of complement regulator Factor H
6ATG 1.8 Å, Insights to complement factor H recruitment by the borrelial CspZ protein as revealed by…
9MLU 1.82 Å, FbaA with Factor H 6-7 domain
9MMX 1.9 Å, M6 protein with Factor H 6-7 domain
3KXV 2.0 Å, Structure of complement Factor H variant Q1139A
3OXU 2.1 Å, Complement components factor H CCP19-20 and C3d in complex
4ONT 2.15 Å, Ternary host recognition complex of complement factor H, C3d, and sialic acid
6ZH1 2.2 Å, Crystal structure of complex between FH19-20 and FhbA protein from Borrelia hermsii
4ZH1 2.24 Å, Complement factor H in complex with the GM1 glycan

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