6F1C: C1rC1s complex

C1rC1s complex. Determined by X-ray diffraction at 4.2 Å resolution. Released 17 Jan 2018.

Method: X-ray diffraction
Resolution: 4.2 Å
Organism: Homo sapiens
Chains: 4
Atoms: 9,260
Mol. weight: 132.95 kDa
Ligands: NAG, CA
Released: 17 Jan 2018

Explore 6F1C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6F1C contains 20 α-helices and 104 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: 7 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	10-13	4	1
α-helix	20-22	3
β-strand	25-32	8	2
β-strand	37-46	10	1
β-strand	47	1	3
β-strand	57-62	6	2
β-strand	67-71	5	2
β-strand	74	1	3
β-strand	94-101	8	2
β-strand	117-125	9	1
α-helix	129-131	3
β-strand	147-150	4	4
β-strand	155-158	4	4
β-strand	163-165	3	5
β-strand	172-174	3	5
β-strand	179-181	3	6
β-strand	186-189	4	7
α-helix	196-198	3
β-strand	202-208	7	6
α-helix	209-210	2
β-strand	213-219	7	7
α-helix	220	1
α-helix	222	1
β-strand	224	1	8
β-strand	237-242	6	6
β-strand	245-250	6	6
α-helix	255-258	4
β-strand	259-260	2	7
β-strand	265-271	7	6
β-strand	280	1	8
β-strand	282-289	8	7

Chain B: 3 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	5-9	5	26
α-helix	16-18	3
β-strand	21-28	8	27
β-strand	33-43	11	26
α-helix	48-50	3
β-strand	54-59	6	27
β-strand	62-67	6	27
β-strand	70-71	2	26
β-strand	82-86	5	26
β-strand	90-97	8	27
β-strand	107-116	10	26
β-strand	131-135	5	28
β-strand	138-142	5	28
β-strand	147-149	3	29
β-strand	156-158	3	29
β-strand	164-165	2	30
β-strand	170-173	4	31
α-helix	180-182	3
β-strand	186-192	7	30
β-strand	197-202	6	31
β-strand	208-210	3	32
β-strand	213	1	33
β-strand	219	1	33
β-strand	222-227	6	30
β-strand	230-235	6	30
β-strand	237-238	2	32
β-strand	245-247	3	31
β-strand	252-258	7	30
β-strand	267-268	2	32
β-strand	269-276	8	31

Chain C: 7 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	9-13	5	9
α-helix	20-22	3
β-strand	25-32	8	10
β-strand	37-46	10	9
β-strand	47	1	11
β-strand	58-63	6	10
β-strand	67-71	5	10
β-strand	72	1	12
β-strand	74	1	11
β-strand	81	1	12
β-strand	94-101	8	10
β-strand	117-125	9	9
α-helix	128-132	5
β-strand	147-150	4	13
β-strand	155-158	4	13
β-strand	163-165	3	14
β-strand	172-174	3	14
β-strand	179-181	3	15
β-strand	186-189	4	16
α-helix	196-198	3
β-strand	202-208	7	15
α-helix	209-210	2
β-strand	213-219	7	16
α-helix	220	1
α-helix	222	1
β-strand	224	1	17
β-strand	237-242	6	15
β-strand	245-250	6	15
α-helix	255-258	4
β-strand	259-260	2	16
β-strand	265-271	7	15
β-strand	280	1	17
β-strand	282-289	8	16

Chain D: 3 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	5-9	5	18
α-helix	16-18	3
β-strand	21-28	8	19
β-strand	33-43	11	18
α-helix	48-50	3
β-strand	54-59	6	19
β-strand	62-67	6	19
β-strand	70-71	2	18
β-strand	82-86	5	18
β-strand	90-97	8	19
β-strand	107-116	10	18
β-strand	131-135	5	20
β-strand	138-142	5	20
β-strand	147-149	3	21
β-strand	156-158	3	21
β-strand	164-165	2	22
β-strand	170-173	4	23
α-helix	180-182	3
β-strand	186-192	7	22
β-strand	198-202	5	23
β-strand	208-210	3	24
β-strand	213	1	25
β-strand	219	1	25
β-strand	222-227	6	22
β-strand	230-235	6	22
β-strand	237-238	2	24
β-strand	245-247	3	23
β-strand	252-258	7	22
β-strand	267-268	2	24
β-strand	269-275	7	23

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement C1r subcomponent	A, C	protein	291	Homo sapiens	P00736 (AlphaFold model)
Complement C1s subcomponent	B, D	protein	277	Homo sapiens	P09871 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>6F1C_1 Complement C1r subcomponent (chains A, C)
SIPIPQKLFGEVTSPLFPKPYPNNFETTTVITVPTGYRVKLVFQQFDLEPSEGCFYDYVK
ISADKKSLGRFCGQLGSPLGNPPGKKEFMSQGNKMLLTFHTDFSNEENGTIMFYKGFLAY
YQAVDLDECASRSKSGEEDPQPQCQHLCHNYVGGYFCSCRPGYELQEDTHSCQAECSSEL
YTEASGYISSLEYPRSYPPDLRCNYSIRVERGLTLHLKFLEPFDIDDHQQVHCPYDQLQI
YANGKNIGEFCGKQRPPDLDTSSNAVDLLFFTDESGDSRGWKLRYTTEIIK

Sequence of entity 2 (B, D), FASTA

>6F1C_2 Complement C1s subcomponent (chains B, D)
EPTMYGEILSPNYPQAYPSEVEKSWDIEVPEGYGIHLYFTHLDIELSENCAYDSVQIISG
DTEEGRLCGQRSSNNPHSPIVEEFQVPYNKLQVIFKSDFSNEERFTGFAAYYVATDINEC
TDFVDVPCSHFCNNFIGGYFCSCPPEYFLHDDMKNCGVNCSGDVFTALIGEIASPNYPKP
YPENSRCEYQIRLEKGFQVVVTLRREDFDVEAADSAGNCLDSLVFVAGDRQFGPYCGHGF
PGPLNIETKSNALDIIFQTDLTGQKKGWKLRYHGDPM

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	2
CA	Calcium ion	Ca	12

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

Primary citation

Structure of the C1r-C1s interaction of the C1 complex of complement activation. Almitairi, J.O.M., Venkatraman Girija, U., Furze, C.M. et al. Proc Natl Acad Sci U S A (2018) 115:768-773. DOI 10.1073/pnas.1718709115 · PubMed

Other PDB entries of the same protein (UniProt P00736 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6F1D 1.95 Å, CUB2 domain of C1r
2QY0 2.6 Å, Active dimeric structure of the catalytic domain of C1r reveals enzyme-product like…
1MD8 2.8 Å, Monomeric structure of the active catalytic domain of complement protease C1r
1GPZ 2.9 Å, The crystal structure of the zymogen catalytic domain of complement protease C1R
9EKE 3.1 Å, Structure of a C1r Zymogen Fragment Bound to SALO, Y51F Mutant
1MD7 3.2 Å, Monomeric structure of the zymogen of complement protease C1r
9EKD 3.28 Å, Structure of a C1r Zymogen Fragment Bound to SALO
7MZT 4.07 Å, Borrelia burgdorferi BBK32-C in complex with an autolytic fragment of human C1r at 4.1A
6F1H 4.5 Å, C1rC1s complex
6F39 5.8 Å, C1r homodimer CUB1-EGF-CUB2
1APQ Structure of the egf-like module of human C1R, NMR, 19 structures

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