6DLW: Complement component polyC9

Complement component polyC9. Determined by electron microscopy at 3.9 Å resolution. Released 12 Sept 2018.

Method: Electron microscopy
Resolution: 3.9 Å
Organism: Homo sapiens
Chains: 22
Atoms: 80,410
Mol. weight: 1352.08 kDa
Ligands: BMA, NAG
Released: 12 Sept 2018

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

Secondary structure: helices and β-sheets

6DLW contains 264 α-helices and 528 β-strands across 22 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.

Chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U and V: 12 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	20	1	1
α-helix	25-27	3
β-strand	34	1	2
β-strand	39-42	4	2
β-strand	50-51	2	1
β-strand	63-66	4	2
α-helix	72-74	3
β-strand	84-85	2	3
β-strand	91-92	2	3
β-strand	138-139	2	4
β-strand	151	1	5
β-strand	162-164	3	6
β-strand	171-173	3	6
β-strand	178-180	3	7
β-strand	186-215	30	8
β-strand	252-281	30	8
β-strand	285-287	3	7
β-strand	294	1	5
α-helix	296-303	8
α-helix	311-320	10
β-strand	324-325	2	4
β-strand	328-329	2	7
β-strand	335-363	29	8
β-strand	380-408	29	8
α-helix	413-424	12
α-helix	428-430	3
α-helix	433-440	8
β-strand	454	1	4
α-helix	455-457	3
α-helix	466-483	18
α-helix	486-488	3
α-helix	490-492	3
α-helix	496	1
β-strand	497-499	3	9
β-strand	504-505	2	1
β-strand	506-508	3	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement component C9	A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V	protein	538	Homo sapiens	P02748 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V), FASTA

>6DLW_1 Complement component C9 (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V)
QYTTSYDPELTESSGSASHIDCRMSPWSEWSQCDPCLRQMFRSRSIEVFGQFNGKRCTDA
VGDRRQCVPTEPCEDAEDDCGNDFQCSTGRCIKMRLRCNGDNDCGDFSDEDDCESEPRPP
CRDRVVEESELARTAGYGINILGMDPLSTPFDNEFYNGLCNRDRDGNTLTYYRRPWNVAS
LIYETKGEKNFRTEHYEEQIEAFKSIIQEKTSNFNAAISLKFTPTETNKAEQCCEETASS
ISLHGKGSFRFSYSKNETYQLFLSYSSKKEKMFLHVKGEIHLGRFVMRNRDVVLTTTFVD
DIKALPTTYEKGEYFAFLETYGTHYSSSGSLGGLYELIYVLDKASMKRKGVELKDIKRCL
GYHLDVSLAFSEISVGAEFNKDDCVKRGEGRAVNITSENLIDDVVSLIRGGTRKYAFELK
EKLLRGTVIDVTDFVNWASSINDAPVLISQKLSPIYNLVPVKMKNAHLKKQNLERAIEDY
INEFSVRKCHTCQNGGTVILMDGKCLCACPFKFEGIACEISKQKISEGLPALEFPNEK

Ligands and cofactors

ID	Name	Formula	Copies
BMA	beta-D-mannopyranose	C6 H12 O6	22
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	22

Primary citation

The first transmembrane region of complement component-9 acts as a brake on its self-assembly. Spicer, B.A., Law, R.H.P., Caradoc-Davies, T.T. et al. Nat Commun (2018) 9:3266-3266. DOI 10.1038/s41467-018-05717-0 · PubMed

Other PDB entries of the same protein (UniProt P02748 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8DE6 3.2 Å, Oligomeric C9 in complex with aE11 Fab
7NYD 3.27 Å, cryoEM structure of 2C9-sMAC
8B0G 3.3 Å, 2C9, C5b9-CD59 structure
8B0H 3.3 Å, 2C9, C5b9-CD59 cryoEM structure
7NYC 3.54 Å, cryoEM structure of 3C9-sMAC
6H03 5.6 Å, Open conformation of the membrane attack complex
6H04 5.6 Å, Closed conformation of the Membrane Attack Complex
5FMW 6.7 Å, The poly-C9 component of the Complement Membrane Attack Complex

Browse structure collections

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