3T5O: Human Complement Component C6

Crystal Structure of human Complement Component C6. Determined by X-ray diffraction at 2.87 Å resolution. Released 1 Feb 2012.

Method: X-ray diffraction
Resolution: 2.87 Å
Organism: Homo sapiens
Chains: 1
Atoms: 6,934
Mol. weight: 104.29 kDa
Ligands: CD, MAN, FUL
Released: 1 Feb 2012

Explore 3T5O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3T5O contains 41 α-helices and 71 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: 41 helices, 71 β-strands

Element	Residues	Length	Sheet
α-helix	3-5	3
α-helix	7	1
β-strand	8	1	1
α-helix	9-14	6
β-strand	21-26	6	2
β-strand	27	1	1
α-helix	33-37	5
α-helix	40-43	4
β-strand	47-52	6	2
α-helix	56-57	2
β-strand	59	1	3
β-strand	62-63	2	4
β-strand	78-79	2	5
β-strand	82	1	6
β-strand	85-87	3	4
β-strand	89-90	2	3
α-helix	93-96	4
β-strand	101	1	6
β-strand	104-105	2	5
β-strand	122-124	3	7
β-strand	130-132	3	7
α-helix	133-135	3
α-helix	147-149	3
α-helix	163	1
β-strand	164-165	2	8
α-helix	166	1
α-helix	169-173	5
β-strand	174-177	4	9
β-strand	182-186	5	9
β-strand	188	1	10
β-strand	199-200	2	8
α-helix	208	1
β-strand	209-210	2	8
β-strand	215-219	5	11
α-helix	226-228	3
β-strand	229-234	6	11
α-helix	237-241	5
α-helix	277-286	10
β-strand	290-306	17	11
β-strand	313	1	10
α-helix	315-320	6
α-helix	330-340	11
β-strand	343-344	2	9
β-strand	347-361	15	11
α-helix	362-368	7
α-helix	372-386	15
α-helix	397-399	3
α-helix	405-408	4
α-helix	413-415	3
β-strand	418-421	4	11
β-strand	424	1	11
α-helix	428-434	7
α-helix	445-457	13
β-strand	460-465	6	11
β-strand	468	1	9
α-helix	469-472	4
α-helix	479-495	17
α-helix	499-501	3
α-helix	503-504	2
β-strand	505	1	12
β-strand	509	1	12
β-strand	510-514	5	3
β-strand	517-521	5	3
α-helix	522-523	2
β-strand	526	1	13
β-strand	534	1	13
β-strand	543	1	14
α-helix	552-557	6
β-strand	561-565	5	15
β-strand	574	1	14
β-strand	585-589	5	15
α-helix	605-607	3
β-strand	623	1	16
α-helix	624-626	3
α-helix	628-629	2
β-strand	632-634	3	17
β-strand	641	1	16
β-strand	646-648	3	18
β-strand	649-651	3	17
β-strand	655-658	4	19
β-strand	662-665	4	18
β-strand	671-672	2	18
β-strand	677-680	4	19
α-helix	681	1
β-strand	682-684	3	20
β-strand	693	1	21
β-strand	700-702	3	20
β-strand	706-708	3	22
β-strand	710	1	21
β-strand	716-717	2	23
β-strand	722-724	3	22
β-strand	726	1	24
β-strand	729	1	24
β-strand	740-741	2	23
β-strand	756-757	2	25
β-strand	764-765	2	25
α-helix	766-767	2
α-helix	768-771	4
β-strand	778-783	6	26
β-strand	788-793	6	26
α-helix	794-801	8
α-helix	804-806	3
β-strand	808-813	6	26
α-helix	820-830	11
β-strand	851-852	2	27
β-strand	859-860	2	27
β-strand	873	1	28
β-strand	876-878	3	29
β-strand	885-886	2	29
β-strand	889	1	28
α-helix	890-899	10
β-strand	904-907	4	29

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement component C6	A	protein	913	Homo sapiens	P13671 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3T5O_1 Complement component C6 (chains A)
CFCDHYAWTQWTSCSKTCNSGTQSRHRQIVVDKYYQENFCEQICSKQETRECNWQRCPIN
CLLGDFGPWSDCDPCIEKQSKVRSVLRPSQFGGQPCTAPLVAFQPCIPSKLCKIEEADCK
NKFRCDSGRCIARKLECNGENDCGDNSDERDCGRTKAVCTRKYNPIPSVQLMGNGFHFLA
GEPRGEVLDNSFTGGICKTVKSSRTSNPYRVPANLENVGFEVQTAEDDLKTDFYKDLTSL
GHNENQQGSFSSQGGSSFSVPIFYSSKRSENINHNSAFKQAIQASHKKDSSFIRIHKVMK
VLNFTTKAKDLHLSDVFLKALNHLPLEYNSALYSRIFDDFGTHYFTSGSLGGVYDLLYQF
SSEELKNSGLTEEEAKHCVRIETKKRVLFAKKTKVEHRCTTNKLSEKHEGSFIQGAEKSI
SLIRGGRSEYGAALAWEKGSSGLEEKTFSEWLESVKENPAVIDFELAPIVDLVRNIPCAV
TKRNNLRKALQEYAAKFDPCQCAPCPNNGRPTLSGTECLCVCQSGTYGENCEKQSPDYKS
NAVDGQWGCWSSWSTCDATYKRSRTRECNNPAPQRGGKRCEGEKRQEEDCTFSIMENNGQ
PCINDDEEMKEVDLPEIEADSGCPQPVPPENGFIRNEKQLYLVGEDVEISCLTGFETVGY
QYFRCLPDGTWRQGDVECQRTECIKPVVQEVLTITPFQRLYRIGESIELTCPKGFVVAGP
SRYTCQGNSWTPPISNSLTCEKDTLTKLKGHCQLGQKQSGSECICMSPEEDCSHHSEDLC
VFDTDSNDYFTSPACKFLAEKCLNNQQLHFLHIGSCQDGRQLEWGLERTRLSSNSTKKES
CGYDTCYDWEKCSASTSKCVCLLPPQCFKGGNQLYCVKMGSSTSEKTLNICEVGTIRCAN
RKMEILHPGKCLA

Ligands and cofactors

ID	Name	Formula	Copies
CD	Cadmium ion	Cd	1
MAN	alpha-D-mannopyranose	C6 H12 O6	4
FUL	beta-L-fucopyranose	C6 H12 O5	1

Primary citation

Structure of Complement C6 Suggests a Mechanism for Initiation and Unidirectional, Sequential Assembly of Membrane Attack Complex (MAC). Aleshin, A.E., Schraufstatter, I.U., Stec, B. et al. J Biol Chem (2012) 287:10210-10222. DOI 10.1074/jbc.M111.327809 · PubMed

Other PDB entries of the same protein (UniProt P13671 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7Q6C 2.29 Å, complement C6 FIM1-2 bound to CP010 antibody
8B0F 3.0 Å, CryoEM structure of C5b8-CD59
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
4A5W 3.5 Å, Crystal structure of C5b6
7NYC 3.54 Å, cryoEM structure of 3C9-sMAC
4E0S 4.21 Å, Crystal Structure of C5b-6
6H03 5.6 Å, Open conformation of the membrane attack complex
6H04 5.6 Å, Closed conformation of the Membrane Attack Complex

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