4LOS: C1s CUB2-CCP1

C1s CUB2-CCP1. Determined by X-ray diffraction at 2.0 Å resolution. Released 7 Aug 2013.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,613
Mol. weight: 20.76 kDa
Ligands: CA
Released: 7 Aug 2013

Explore 4LOS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4LOS contains 6 α-helices and 22 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: 6 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	161-165	5	1
β-strand	169-173	5	2
α-helix	180-182	3
β-strand	186-192	7	1
α-helix	193-194	2
β-strand	197-202	6	2
α-helix	205-207	3
β-strand	208-210	3	3
β-strand	222-227	6	1
β-strand	230-235	6	1
β-strand	237-238	2	3
β-strand	245-247	3	2
β-strand	252-258	7	1
β-strand	267-268	2	3
β-strand	269-276	8	2
α-helix	277	1
β-strand	278	1	4
α-helix	280-283	4
β-strand	287-290	4	5
β-strand	297	1	4
β-strand	301-306	6	5
α-helix	307	1
β-strand	310-313	4	6
β-strand	319	1	6
β-strand	321-325	5	5
β-strand	326	1	7
β-strand	332	1	7
β-strand	338-341	4	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement C1s subcomponent heavy chain	A	protein	187	Homo sapiens	P09871 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4LOS_1 Complement C1s subcomponent heavy chain (chains A)
GVNCSGDVFTALIGEIASPNYPKPYPENSRCEYQIRLEKGFQVVVTLRREDFDVEAADSA
GNCLDSLVFVAGDRQFGPYCGHGFPGPLNIETKSNALDIIFQTDLTGQKKGWKLRYHGDP
MPCPKEDTPNSVWEPAKAKYVFRDVVQITCLDGFEVVEGRVGATSFYSTCQSNGKWSNSK
LKCQPVD

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	1

Primary citation

Structural basis of the C1q/C1s interaction and its central role in assembly of the C1 complex of complement activation. Venkatraman Girija, U., Gingras, A.R., Marshall, J.E. et al. Proc Natl Acad Sci U S A (2013) 110:13916-13920. DOI 10.1073/pnas.1311113110 · 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
8TYP 1.8 Å, Complement Protease C1s Inhibited by 6-(4-phenylpiperazin-1-yl)pyridine-3-carboximidamide
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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