8TYP: Complement C1s subcomponent

Complement Protease C1s Inhibited by 6-(4-phenylpiperazin-1-yl)pyridine-3-carboximidamide. Determined by X-ray diffraction at 1.8 Å resolution. Released 29 Nov 2023.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,795
Mol. weight: 39.04 kDa
Ligands: SQT
Released: 29 Nov 2023

Explore 8TYP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8TYP contains 14 α-helices and 32 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: 14 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	358	1	1
α-helix	362-364	3
β-strand	368-370	3	2
α-helix	371-373	3
β-strand	377	1	1
β-strand	381-383	3	3
β-strand	384-386	3	2
β-strand	391-393	3	4
β-strand	400-403	4	3
β-strand	409-410	2	3
β-strand	411	1	5
β-strand	415	1	5
α-helix	418-419	2
β-strand	421-423	3	4
α-helix	424-425	2
β-strand	439	1	6
β-strand	442-443	2	7
β-strand	452-456	5	8
β-strand	459-466	8	8
β-strand	469-472	4	8
α-helix	474-477	4
β-strand	485-487	3	8
β-strand	491	1	9
β-strand	501-503	3	8
α-helix	504	1
β-strand	505-510	6	8
α-helix	515-516	2
β-strand	531-535	5	8
α-helix	538-541	4
β-strand	542	1	10
β-strand	545	1	10
α-helix	547-548	2
β-strand	549	1	7
α-helix	550-552	3
α-helix	555-557	3
β-strand	564-569	6	7
β-strand	581	1	9
β-strand	583-590	8	7
α-helix	592-597	6
β-strand	616-620	5	7
β-strand	626	1	6
β-strand	635-639	5	7
β-strand	647-655	9	7
β-strand	662-667	6	7
α-helix	668-671	4
α-helix	672-680	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement C1s subcomponent	A	protein	344	Homo sapiens	P09871 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>8TYP_1 Complement C1s subcomponent (chains A)
AEDCGIPESIENGKVEDPESTLFGSVIRYTCEEPYYYMENGGGGEYHCAGNGSWVNEVLG
PELPKCVPVCGVPREPFEEKQRIIGGSDADIKNFPWQVFFDNPWAGGALINEYWVLTAAH
VVEGNREPTMYVGSTSVQTSRLAKSKMLTPEHVFIHPGWKLLEVPEGRTNFDNDIALVRL
KDPVKMGPTVSPICLPGTSSDYNLMDGDLGLISGWGRTEKRDRAVRLKAARLPVAPLRKC
KEVKVEKPTADAEAYVFTPNMICAGGEKGMDSCKGDSGGAFAVQDPNDKTKFYAAGLVSW
GPQCGTYGLYTRVKNYVDWIMKTMQENSTPREDGSGHHHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
SQT	6-(4-phenylpiperazin-1-yl)pyridine-3-carboximidamide	C16 H19 N5	1

Primary citation

Inhibition of the C1s Protease and the Classical Complement Pathway by 6-(4-Phenylpiperazin-1-yl)Pyridine-3-Carboximidamide and Chemical Analogs. Xu, X., Herdendorf, T.J., Duan, H. et al. J Immunol (2024) 212:689-701. DOI 10.4049/jimmunol.2300630 · PubMed

Other PDB entries of the same protein (UniProt P09871 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1NZI 1.5 Å, Crystal Structure of the CUB1-EGF Interaction Domain of Complement Protease C1s
1ELV 1.7 Å, Crystal structure of the catalytic domain of human complement C1S protease
4LOS 2.0 Å, C1s CUB2-CCP1
4LOR 2.5 Å, C1s CUB1-EGF-CUB2 in complex with a collagen-like peptide from C1q
5UBM 2.5 Å, Crystal structure of human C1s in complex with inhibitor gigastasin
8GMN 2.6 Å, Crystal structure of human C1s in complex with inhibitor
9X1H 2.6 Å, Cryo-EM Structure of human complement C1s CUB domain in complex with RAY121
4J1Y 2.66 Å, The X-ray crystal structure of human complement protease C1s zymogen
4LOT 2.92 Å, C1s CUB2-CCP1-CCP2
4LMF 2.92 Å, C1s CUB1-egf-CUB2
8W18 3.94 Å, The crystal structure of the Michaelis-Menten complex of a C1s/C1-INH at 3.94 Angstroms
6F1C 4.2 Å, C1rC1s complex

Browse structure collections

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