6ATG: HCG40889, isoform CRA_b

Insights to complement factor H recruitment by the borrelial CspZ protein as revealed by structural analysis. Determined by X-ray diffraction at 1.8 Å resolution. Released 12 Sept 2018.

Method: X-ray diffraction
Resolution: 1.8 Å
Organisms: Homo sapiens, Borrelia burgdorferi B31
Chains: 4
Atoms: 5,031
Mol. weight: 63.37 kDa
Ligands: MG
Released: 12 Sept 2018

Explore 6ATG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6ATG contains 30 α-helices and 18 β-strands across 4 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: 2 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	371-372	2	1
α-helix	373-375	3
β-strand	379	1	2
β-strand	387-388	2	1
β-strand	393-395	3	3
β-strand	398	1	2
β-strand	402-403	2	4
α-helix	405-407	3
β-strand	410-414	5	3
β-strand	417-419	3	3
β-strand	425-426	2	4

Chain B: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	23-38	16
α-helix	42-65	24
α-helix	71-82	12
α-helix	83-85	3
α-helix	86-97	12
α-helix	99-101	3
α-helix	104-119	16
α-helix	128-155	28
α-helix	160-179	20
α-helix	181-196	16
α-helix	199-201	3
α-helix	214-232	19

Chain C: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	25-38	14
α-helix	42-65	24
α-helix	71-82	12
α-helix	83-85	3
α-helix	86-98	13
α-helix	107-118	12
α-helix	128-155	28
α-helix	160-179	20
α-helix	181-196	16
α-helix	199-201	3
α-helix	214-229	16

Chain D: 5 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	370	1
β-strand	371-372	2	5
α-helix	373-375	3
β-strand	379	1	6
β-strand	387-388	2	5
β-strand	393-395	3	7
β-strand	398	1	6
β-strand	402-403	2	8
α-helix	405-407	3
β-strand	410-414	5	7
β-strand	417-419	3	7
α-helix	421-422	2
β-strand	425-426	2	8
α-helix	427	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
HCG40889, isoform CRA_b	A, D	protein	61	Homo sapiens	P08603 (AlphaFold model)
Complement regulator-acquiring surface protein 2 (CRASP-2)	B, C	protein	214	Borrelia burgdorferi B31	O50665 (AlphaFold model)

Sequence of entity 1 (A, D), FASTA

>6ATG_1 HCG40889, isoform CRA_b (chains A, D)
HMKCYFPYLENGYNQNHGRKFVQGKSIDVACHPGYALPKAQTTVTCMENGWSPTPRCIRV
K

Sequence of entity 2 (B, C), FASTA

>6ATG_2 Complement regulator-acquiring surface protein 2 (CRASP-2) (chains B, C)
GHMNQRNINELKIFVEKAKYYSIKLDAIYNECTGAYNDIMTYSEGTFSDQSKVNQAISIF
KKDNKIVNKFKELEKIIEEYKPMFLSKLIDDFAIELDQAVDNDVSNARHVADSYKKLRKS
VVLAYIESFDVISSKFVDSKFVEASKKFVNKAKEFVEENDLIALECIVKTIGDMVNDREI
NSRSRYNNFYKKEADFLGAAVELEGAYKAIKQTL

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2

Primary citation

Insights to complement factor H recruitment by the borrelial CspZ protein as revealed by structural analysis. Liu, A., Yan, H., Wu, Y. et al. To be published.

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…
3SW0 1.8 Å, Structure of the C-terminal region (modules 18-20) of complement regulator Factor H
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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