1ELV: Complement C1S component

Crystal structure of the catalytic domain of human complement C1S protease. Determined by X-ray diffraction at 1.7 Å resolution. Released 14 Mar 2001.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,736
Mol. weight: 37.68 kDa
Ligands: NES
Released: 14 Mar 2001

Explore 1ELV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1ELV contains 12 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: 12 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	343	1	1
α-helix	347-349	3
β-strand	353-355	3	2
α-helix	356-358	3
β-strand	362	1	1
β-strand	366-368	3	3
β-strand	369-371	3	2
β-strand	376-378	3	4
β-strand	385-388	4	3
β-strand	394-395	2	3
β-strand	396	1	5
β-strand	400	1	5
α-helix	403-404	2
β-strand	406-408	3	4
β-strand	424	1	6
β-strand	427-428	2	7
α-helix	431-433	3
β-strand	437-441	5	8
β-strand	444-451	8	8
β-strand	454-457	4	8
α-helix	459-462	4
β-strand	470-471	2	8
β-strand	476	1	9
β-strand	487-488	2	8
β-strand	490-495	6	8
β-strand	516-520	5	8
α-helix	523-526	4
β-strand	527	1	10
β-strand	530	1	10
α-helix	532-533	2
β-strand	534	1	7
α-helix	535-536	2
α-helix	540-542	3
β-strand	549-554	6	7
β-strand	566	1	9
β-strand	568-575	8	7
α-helix	577-581	5
β-strand	601-605	5	7
β-strand	611	1	6
β-strand	620-624	5	7
β-strand	632-640	9	7
β-strand	647-652	6	7
α-helix	653-656	4
α-helix	657-666	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement C1S component	A	protein	333	Homo sapiens	P09871 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1ELV_1 COMPLEMENT C1S COMPONENT (chains A)
DLDCGIPESIENGKVEDPESTLFGSVIRYTCEEPYYYMENGGGGEYHCAGNGSWVNEVLG
PELPKCVPVCGVPREPFEEKQRIIGGSDADIKNFPWQVFFDNPWAGGALINEYWVLTAAH
VVEGNREPTMYVGSTSVQTSRLAKSKMLTPEHVFIHPGWKLLAVPEGRTNFDNDIALVRL
KDPVKMGPTVSPICLPGTSSDYNLMDGDLGLISGWGRTEKRDRAVRLKAARLPVAPLRKC
KEVKVEKPTADAEAYVFTPNMICAGGEKGMDSCKGDSGGAFAVQDPNDKTKFYAAGLVSW
GPQCGTYGLYTRVKNYVDWIMKTMQENSTPRED

Ligands and cofactors

ID	Name	Formula	Copies
NES	2-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-ethanesulfonic acid	C6 H15 N O6 S	1

Water and common crystallization additives (SO4) are not listed.

Primary citation

Crystal structure of the catalytic domain of human complement c1s: a serine protease with a handle. Gaboriaud, C., Rossi, V., Bally, I. et al. EMBO J (2000) 19:1755-1765. DOI 10.1093/emboj/19.8.1755 · 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
8TYP 1.8 Å, Complement Protease C1s Inhibited by 6-(4-phenylpiperazin-1-yl)pyridine-3-carboximidamide
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

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