6RPT: Tick complement inhibitor CirpT1

Structure of tick complement inhibitor CirpT1 complexed with macroglobubulin domain 4 of human complement C5. Determined by X-ray diffraction at 2.7 Å resolution. Released 8 Jan 2020.

Method: X-ray diffraction
Resolution: 2.7 Å
Organisms: Homo sapiens, Rhipicephalus pulchellus
Chains: 6
Atoms: 4,658
Mol. weight: 80.85 kDa
Released: 8 Jan 2020

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

Secondary structure: helices and β-sheets

6RPT contains 11 α-helices and 66 β-strands across 6 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, 11 β-strands

Element	Residues	Length	Sheet
β-strand	353-356	4	8
β-strand	362-363	2	9
α-helix	364	1
β-strand	369-376	8	8
β-strand	382	1	8
β-strand	387-396	10	9
β-strand	401-403	3	9
α-helix	404-406	3
β-strand	407-410	4	9
β-strand	417-422	6	8
β-strand	428-437	10	9
β-strand	449-456	8	9
β-strand	458	1	7

Chains B and D: 1 helix, 10 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	10
β-strand	15-17	3	11
β-strand	20-23	4	11
β-strand	26-29	4	11
β-strand	33-35	3	10
β-strand	42-46	5	10
β-strand	51-55	5	10
α-helix	56-59	4
β-strand	60-61	2	8
β-strand	67-69	3	12
β-strand	82-84	3	12

Chains C and E: 3 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	348	1	13
β-strand	350	1	13
β-strand	353-356	4	14
β-strand	362-363	2	15
α-helix	364	1
β-strand	369-376	8	14
β-strand	382	1	14
β-strand	387-396	10	15
β-strand	401-403	3	15
α-helix	404-406	3
β-strand	407-410	4	15
β-strand	417-422	6	14
β-strand	428-437	10	15
α-helix	444-446	3
β-strand	449-456	8	15

Chain F: 1 helix, 11 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	4
β-strand	15-17	3	5
β-strand	20-23	4	5
β-strand	26-29	4	5
β-strand	33-35	3	4
β-strand	42-46	5	4
β-strand	51-55	5	4
α-helix	56-59	4
β-strand	60-61	2	2
β-strand	67-69	3	6
β-strand	70	1	7
β-strand	82-84	3	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement C5	A, C, E	protein	133	Homo sapiens	P01031 (AlphaFold model)
Putative 8.9 kDa family member	B, D, F	protein	113	Rhipicephalus pulchellus	L7MB58 (AlphaFold model)

Sequence of entity 1 (A, C, E), FASTA

>6RPT_1 Complement C5 (chains A, C, E)
MKHHHHHHSAGLEVLFQGPMVLSPYKLNLVATPLFLKPGIPYPIKVQVKDSLDQLVGGVP
VTLNAQTIDVNQETSDLDPSKSVTRVDDGVASFVLNLPSGVTVLEFNVKTDAPDLPEENQ
AREGYRAIAYSSL

Sequence of entity 2 (B, D, F), FASTA

>6RPT_2 Putative 8.9 kDa family member (chains B, D, F)
MKHHHHHHSAGLEVLFQGPMGDVQERGHTYVTKNVTVEDGACVYLRNVIPNGETKALNNP
CVLSTCYAADRKVNSTLCPNIGVDEGCHVEWTPDGVYPNCCPKHVCPSATASS

Primary citation

An inhibitor of complement C5 provides structural insights into activation. Reichhardt, M.P., Johnson, S., Tang, T. et al. Proc Natl Acad Sci U S A (2020) 117:362-370. DOI 10.1073/pnas.1909973116 · PubMed

Other PDB entries of the same protein (UniProt P01031 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9Y6C 2.0 Å, X-ray structure analysis of human Complement Component 5 TE domain in complex with the…
5B71 2.11 Å, Crystal structure of complement C5 in complex with SKY59
4UU9 2.12 Å, Crystal structure of the human c5a in complex with MEDI7814 a neutralising antibody
7AD7 2.3 Å, Crystal structure of human complement C5 in complex with the K8 bovine knob domain…
5B4P 2.4 Å, Complex structure of human C5a and its binding repebody
4P39 2.4 Å, Crystal structure of the human C5aR antagonist C5a-A8
7OP0 2.57 Å, Crystal structure of complement C5 in complex with chemically synthesized K92 knob domain.
3HQA 2.59 Å, Crystal structure of human desarg-C5A
5HCC 2.59 Å, Ternary complex of human Complement C5 with Ornithodoros moubata OmCI and Dermacentor…
22GM 2.7 Å, C5a bound C5aR1 in complex with beta-arrestin1
7AD6 2.75 Å, Crystal structure of human complement C5 in complex with the K92 bovine knob domain…
22GK 2.84 Å, C5a bound C5aR2 in complex with beta-arrestin1

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