3SW0: Complement factor H

Structure of the C-terminal region (modules 18-20) of complement regulator Factor H. Determined by X-ray diffraction at 1.8 Å resolution. Released 14 Mar 2012.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,770
Mol. weight: 21.89 kDa
Ligands: PO4
Released: 14 Mar 2012

Explore 3SW0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3SW0 contains 11 α-helices and 30 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 X: 11 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	1048	1	1
α-helix	1051-1053	3
β-strand	1057-1059	3	2
α-helix	1062-1063	2
β-strand	1067	1	1
β-strand	1072-1074	3	3
β-strand	1075-1077	3	2
α-helix	1078	1
α-helix	1081	1
β-strand	1082-1084	3	4
β-strand	1088-1090	3	3
β-strand	1091-1092	2	5
β-strand	1095-1096	2	5
β-strand	1101-1103	3	4
β-strand	1109	1	6
α-helix	1112-1114	3
β-strand	1118-1120	3	7
β-strand	1128	1	6
β-strand	1133-1135	3	8
β-strand	1136-1138	3	7
α-helix	1139	1
β-strand	1143-1145	3	9
β-strand	1149-1151	3	8
β-strand	1152-1153	2	10
β-strand	1156-1157	2	10
α-helix	1158-1161	4
β-strand	1162-1164	3	9
α-helix	1165-1166	2
β-strand	1167-1168	2	11
α-helix	1171-1177	7
β-strand	1179-1181	3	12
β-strand	1190-1191	2	11
β-strand	1196-1198	3	13
β-strand	1199-1201	3	12
β-strand	1206-1207	2	14
α-helix	1211-1213	3
β-strand	1215-1217	3	13
β-strand	1219	1	15
β-strand	1222	1	15
α-helix	1224-1226	3
β-strand	1228-1229	2	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement factor H	X	protein	188	Homo sapiens	P08603 (AlphaFold model)

Sequence of entity 1 (X), FASTA

>3SW0_1 Complement factor H (chains X)
AGTSCVNPPTVQNAYIVSRQMSKYPSGERVRYQCRSPYEMFGDEEVMCLNGNWTEPPQCK
DSTGKCGPPPPIDNGDITSFPLSVYAPASSVEYQCQNLYQLEGNKRITCRNGQWSEPPKC
LHPCVISREIMENYNIALRWTAKQKLYSRTGESVEFVCKRGYRLSSRSHTLRTTCWDGKL
EYPTCAKR

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	1

Water and common crystallization additives (GOL) are not listed.

Primary citation

Structural Analysis of the C-Terminal Region (Modules 18-20) of Complement Regulator Factor H (FH). Morgan, H.P., Mertens, H.D., Guariento, M. et al. PLoS One (2012) 7:e32187-e32187. DOI 10.1371/journal.pone.0032187 · 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
2G7I 1.75 Å, Structure of Human Complement Factor H Carboxyl Terminal Domains 19-20: a Basis for…
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

Browse structure collections

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