4LMF: C1s CUB1-egf-CUB2

C1s CUB1-egf-CUB2. Determined by X-ray diffraction at 2.92 Å resolution. Released 7 Aug 2013.

Method: X-ray diffraction
Resolution: 2.92 Å
Organism: Homo sapiens
Chains: 4
Atoms: 8,768
Mol. weight: 125.03 kDa
Ligands: CA
Released: 7 Aug 2013

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

Secondary structure: helices and β-sheets

4LMF contains 17 α-helices and 101 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: 4 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	5-9	5	1
α-helix	16-18	3
β-strand	21-28	8	2
β-strand	33-44	12	1
α-helix	48-50	3
β-strand	54-59	6	2
β-strand	62-67	6	2
β-strand	69-71	3	1
β-strand	82-86	5	1
β-strand	90-97	8	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	161-165	5	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	208-209	2	7
β-strand	222-227	6	5
β-strand	230-235	6	5
β-strand	238	1	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: 4 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	5-9	5	8
α-helix	16-18	3
β-strand	22-28	7	9
β-strand	33-44	12	8
α-helix	48-50	3
β-strand	54-59	6	9
β-strand	62-67	6	9
β-strand	69-71	3	8
β-strand	82-86	5	8
β-strand	90-96	7	9
β-strand	107-116	10	8
β-strand	131-135	5	10
β-strand	138-142	5	10
β-strand	147-149	3	11
β-strand	156-158	3	11
β-strand	161-165	5	12
β-strand	169-173	5	13
α-helix	180-182	3
β-strand	186-192	7	12
β-strand	197-202	6	13
α-helix	205-207	3
β-strand	208-209	2	14
β-strand	222-227	6	12
β-strand	230-235	6	12
β-strand	238	1	14
β-strand	245-247	3	13
β-strand	252-258	7	12
β-strand	267-268	2	14
β-strand	269-276	8	13

Chain C: 4 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	5-9	5	15
α-helix	16-18	3
β-strand	21-28	8	16
β-strand	33-43	11	15
α-helix	48-50	3
β-strand	54-59	6	16
β-strand	62-67	6	16
β-strand	70	1	15
β-strand	82-86	5	15
β-strand	90-97	8	16
β-strand	107-116	10	15
β-strand	131-135	5	17
β-strand	138-142	5	17
β-strand	148-149	2	18
β-strand	156-157	2	18
β-strand	161-165	5	19
β-strand	169-173	5	20
α-helix	180-182	3
β-strand	186-192	7	19
β-strand	197-202	6	20
α-helix	205-207	3
β-strand	208-209	2	21
β-strand	222-227	6	19
β-strand	230-235	6	19
β-strand	238	1	21
β-strand	245-247	3	20
β-strand	252-258	7	19
β-strand	267-268	2	21
β-strand	269-276	8	20

Chain D: 5 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	5-9	5	22
α-helix	16-18	3
β-strand	21-28	8	23
β-strand	33-43	11	22
α-helix	48-50	3
β-strand	54-59	6	23
β-strand	62-67	6	23
β-strand	70	1	22
β-strand	82-86	5	22
β-strand	90-97	8	23
β-strand	107-116	10	22
β-strand	131-135	5	24
β-strand	138-142	5	24
β-strand	147-149	3	25
β-strand	156-158	3	25
β-strand	161-165	5	26
β-strand	169-173	5	27
α-helix	180-182	3
β-strand	186-192	7	26
α-helix	193-194	2
β-strand	195	1	27
β-strand	197-202	6	27
α-helix	205-207	3
β-strand	208-209	2	28
β-strand	222-227	6	26
β-strand	230-235	6	26
β-strand	238	1	28
β-strand	245-247	3	27
β-strand	252-258	7	26
β-strand	267-268	2	28
β-strand	269-276	8	27

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement C1s subcomponent heavy chain	A, B, C, D	protein	276	Homo sapiens	P09871 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>4LMF_1 Complement C1s subcomponent heavy chain (chains A, B, C, D)
PTMYGEILSPNYPQAYPSEVEKSWDIEVPEGYGIHLYFTHLDIELSENCAYDSVQIISGD
TEEGRLCGQRSSNNPHSPIVEEFQVPYNKLQVIFKSDFSNEERFTGFAAYYVATDINECT
DFVDVPCSHFCNNFIGGYFCSCPPEYFLHDDMKNCGVNCSGDVFTALIGEIASPNYPKPY
PENSRCEYQIRLEKGFQVVVTLRREDFDVEAADSAGNCLDSLVFVAGDRQFGPYCGHGFP
GPLNIETKSNALDIIFQTDLTGQKKGWKLRYHGDPM

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	12

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
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
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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