2QQH: Complement component C8 alpha chain

Structure of C8a-MACPF reveals mechanism of membrane attack in complement immune defense. Determined by X-ray diffraction at 2.5 Å resolution. Released 25 Sept 2007.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,462
Mol. weight: 37.89 kDa
Ligands: NI
Released: 25 Sept 2007

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

Secondary structure: helices and β-sheets

2QQH contains 17 α-helices and 18 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: 17 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	103	1	1
β-strand	106	1	2
β-strand	108	1	2
α-helix	114	1
β-strand	115	1	3
α-helix	116	1
α-helix	119-122	4
β-strand	124-126	3	4
β-strand	133-136	4	4
β-strand	138	1	5
β-strand	148	1	1
β-strand	149-151	3	3
β-strand	175-177	3	3
β-strand	182-193	12	4
α-helix	203-213	11
α-helix	216-218	3
β-strand	221-224	4	4
α-helix	229-230	2
β-strand	231-232	2	4
α-helix	239-245	7
α-helix	247-250	4
β-strand	258-273	16	4
β-strand	280	1	5
α-helix	282-289	8
α-helix	297-307	11
β-strand	310-327	18	4
α-helix	329-334	6
α-helix	3-12	10
β-strand	390-394	5	4
α-helix	415-419	5
α-helix	420-422	3
β-strand	425-433	9	4
α-helix	434-438	5
α-helix	445-447	3
α-helix	448-462	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement component C8 alpha chain	A	protein	334	Homo sapiens	P07357 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2QQH_1 Complement component C8 alpha chain (chains A)
GSVRAIDEDCSQYEPIPGSQKAALGYNILTQEDAQSVYDASYYGGQCETVYNGEWRELRY
DSTSERLYYGDDEKYFRKPYNFLKYHFEALADTGISSEFYDNANDLLSKVKKDKSDSFGV
TIGIGPAGSPLLVGVGVSHSQDTSFLNELNKYNEKKFIFTRIFTKVQTAHFKMRKDDIML
DEGMLQSLMELPDQYNYGMYAKFINDYGTHYITSGSMGGIYEYILVIDKAKMESLGXXXX
XXXXXXXXARKAMAVEDIISRVRGGSSGWSGGLAQNRSTITYRSWGRSLKYNPVVIDFEM
QPIHEVLRHTSLGPLEAKRQNLRRALDQYLMAAA

Ligands and cofactors

ID	Name	Formula	Copies
NI	Nickel (II) ion	Ni	1

Water and common crystallization additives (SO4) are not listed.

Primary citation

Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense. Hadders, M.A., Beringer, D.X., Gros, P. Science (2007) 317:1552-1554. DOI 10.1126/science.1147103 · 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…
2RD7 2.15 Å, Human Complement Membrane Attack Proteins Share a Common Fold with Bacterial Cytolysins
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

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