4LOR: C1s CUB1-EGF-CUB2

C1s CUB1-EGF-CUB2 in complex with a collagen-like peptide from C1q. Determined by X-ray diffraction at 2.5 Å resolution. Released 7 Aug 2013.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,701
Mol. weight: 38.94 kDa
Ligands: NAG, CA
Released: 7 Aug 2013

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

Secondary structure: helices and β-sheets

4LOR contains 11 α-helices and 25 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: 5 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	5-9	5	1
α-helix	16-18	3
β-strand	22-28	7	2
β-strand	33-43	11	1
α-helix	48-50	3
β-strand	54-59	6	2
β-strand	62-67	6	2
β-strand	70-71	2	1
β-strand	82-86	5	1
β-strand	90-96	7	2
β-strand	107-116	10	1
β-strand	131-135	5	3
β-strand	138-142	5	3
β-strand	147-149	3	4
β-strand	156-158	3	4
β-strand	164-165	2	5
β-strand	169-173	5	6
α-helix	180-182	3
β-strand	186-192	7	5
β-strand	197-202	6	6
α-helix	205-207	3
β-strand	208-210	3	7
α-helix	211-213	3
β-strand	222-227	6	5
β-strand	230-235	6	5
β-strand	237-238	2	7
β-strand	245-247	3	6
β-strand	252-258	7	5
β-strand	267-268	2	7
β-strand	269-276	8	6

Chain B: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	6-10	5
α-helix	15-19	5
α-helix	21-23	3

Chain C: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	6-10	5
α-helix	12-19	8

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	3-22	20

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement C1s subcomponent heavy chain	A	protein	276	Homo sapiens	P09871 (AlphaFold model)
collagen-like peptide from C1q	B, C, D	protein	29

Sequence of entity 1 (A), FASTA

>4LOR_1 Complement C1s subcomponent heavy chain (chains A)
PTMYGEILSPNYPQAYPSEVEKSWDIEVPEGYGIHLYFTHLDIELSENCAYDSVQIISGD
TEEGRLCGQRSSNNPHSPIVEEFQVPYNKLQVIFKSDFSNEERFTGFAAYYVATDINECT
DFVDVPCSHFCNNFIGGYFCSCPPEYFLHDDMKNCGVNCSGDVFTALIGEIASPNYPKPY
PENSRCEYQIRLEKGFQVVVTLRREDFDVEAADSAGNCLDSLVFVAGDRQFGPYCGHGFP
GPLNIETKSNALDIIFQTDLTGQKKGWKLRYHGDPM

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

>4LOR_2 collagen-like peptide from C1q (chains B, C, D)
XGPPGPPGPPGPPGKLGPPGPPGPPGPPX

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1
CA	Calcium ion	Ca	3

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

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
4LOS 2.0 Å, C1s CUB2-CCP1
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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