2RD7: Complement component C8 alpha chain

Human Complement Membrane Attack Proteins Share a Common Fold with Bacterial Cytolysins. Determined by X-ray diffraction at 2.15 Å resolution. Released 27 May 2008.

Method: X-ray diffraction
Resolution: 2.15 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,011
Mol. weight: 62.28 kDa
Released: 27 May 2008

Explore 2RD7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2RD7 contains 22 α-helices and 30 β-strands across 2 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: 14 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	114	1
β-strand	115	1	1
α-helix	116	1
α-helix	119-122	4
β-strand	124-127	4	2
β-strand	132-136	5	2
β-strand	138	1	3
β-strand	149-152	4	1
β-strand	158-161	4	4
β-strand	166-169	4	4
β-strand	174-177	4	1
β-strand	182-187	6	2
β-strand	196-200	5	2
α-helix	203-213	11
β-strand	218-222	5	2
β-strand	230-235	6	2
α-helix	243-250	8
β-strand	257-273	17	2
β-strand	278	1	5
β-strand	280	1	3
α-helix	282-289	8
α-helix	297-307	11
β-strand	310-328	19	2
α-helix	329-335	7
α-helix	339-349	11
α-helix	368-372	5
α-helix	378-383	6
β-strand	386-391	6	2
β-strand	394	1	2
α-helix	413-422	10
β-strand	425-433	9	2
α-helix	434-440	7
β-strand	441	1	5
α-helix	447-461	15

Chain C: 8 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	16-18	3
β-strand	29-38	10	6
α-helix	41-44	4
β-strand	54-58	5	6
β-strand	65-72	8	6
β-strand	75-82	8	6
β-strand	91-94	4	6
α-helix	100-102	3
β-strand	103-110	8	6
β-strand	115-121	7	6
β-strand	127-132	6	6
α-helix	137-138	2
α-helix	139-151	13
α-helix	156-158	3
β-strand	159-161	3	6
α-helix	162-163	2
α-helix	173-175	3
β-strand	176-178	3	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement component C8 alpha chain	A	protein	367	Homo sapiens	P07357 (AlphaFold model)
Complement component C8 gamma chain	C	protein	184	Homo sapiens	P07360 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2RD7_1 Complement component C8 alpha chain (chains A)
HHHHHHMVRAIDEDCSQYEPIPGSQKAALGYNILTQEDAQSVYDASYYGGQCETVYNGEW
RELRYDSTCERLYYGDDEKYFRKPYNFLKYHFEALADTGISSEFYDNANDLLSKVKKDKS
DSFGVTIGIGPAGSPLLVGVGVSHSQDTSFLNELNKYNEKKFIFTRIFTKVQTAHFKMRK
DDIMLDEGMLQSLMELPDQYNYGMYAKFINDYGTHYITSGSMGGIYEYILVIDKAKMESL
GITSRDITTCFGGSLGIQYEDKINVGGGLSGDHCKKFGGGKTERARKAMAVEDIISRVRG
GSSGWSGGLAQNRSTITYRSWGRSLKYNPVVIDFEMQPIHEVLRHTSLGPLEAKRQNLRR
ALDQYLM

Sequence of entity 2 (C), FASTA

>2RD7_2 Complement component C8 gamma chain (chains C)
MAQKPQRPRRPASPISTIQPKANFDAQQFAGTWLLVAVGSACRFLQEQGHRAEATTLHVA
PQGTAMAVSTFRKLDGICWQVRQLYGDTGVLGRFLLQARDARGAVHVVVAETDYQSFAVL
YLERAGQLSVKLYARSLPVSDSVLSGFEQRVQEAHLTEDQIFYFPKYGFCEAADQFHVLD
EVRR

Primary citation

Structure of human C8 protein provides mechanistic insight into membrane pore formation by complement. Lovelace, L.L., Cooper, C.L., Sodetz, J.M. et al. J Biol Chem (2011) 286:17585-17592. DOI 10.1074/jbc.M111.219766 · PubMed

Other PDB entries of the same protein (UniProt P07357 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2QOS 1.81 Å, Crystal structure of complement protein C8 in complex with a peptide containing the C8…
2QQH 2.5 Å, Structure of C8a-MACPF reveals mechanism of membrane attack in complement immune defense
3OJY 2.51 Å, Crystal Structure of Human Complement Component C8
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
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

Browse structure collections

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