3OJY: Human Complement Component C8

Crystal Structure of Human Complement Component C8. Determined by X-ray diffraction at 2.51 Å resolution. Released 13 Apr 2011.

Method: X-ray diffraction
Resolution: 2.51 Å
Organism: Homo sapiens
Chains: 3
Atoms: 9,234
Mol. weight: 144.92 kDa
Ligands: BMA, CA
Released: 13 Apr 2011

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

Secondary structure: helices and β-sheets

3OJY contains 56 α-helices and 75 β-strands across 3 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: 27 helices, 30 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
β-strand	10-11	2	1
α-helix	13-20	8
β-strand	26-30	5	2
β-strand	33-35	3	1
β-strand	37	1	3
α-helix	41-43	3
β-strand	49-53	5	2
β-strand	70-71	2	4
β-strand	78-79	2	4
α-helix	81-83	3
α-helix	114	1
β-strand	115	1	5
α-helix	116	1
α-helix	119-122	4
β-strand	124-127	4	6
β-strand	132-136	5	6
β-strand	138	1	7
β-strand	148-151	4	5
β-strand	159-161	3	8
α-helix	162-164	3
β-strand	166-168	3	8
α-helix	171-173	3
β-strand	175-178	4	5
β-strand	182-187	6	6
α-helix	188-190	3
β-strand	196-200	5	6
α-helix	203-210	8
α-helix	247-249	3
β-strand	257-273	17	6
β-strand	278	1	9
α-helix	279	1
β-strand	280	1	7
α-helix	281	1
α-helix	282-289	8
α-helix	297-307	11
β-strand	310-328	19	6
α-helix	329-334	6
α-helix	339-348	10
α-helix	378-383	6
β-strand	386-391	6	6
β-strand	394	1	6
α-helix	413-419	7
α-helix	420-422	3
β-strand	425-433	9	6
α-helix	434-440	7
β-strand	441	1	9
α-helix	447-463	17
α-helix	466-468	3
α-helix	476-477	2
β-strand	478-481	4	3
β-strand	484-487	4	3
α-helix	512-515	4
β-strand	519	1	10
α-helix	520-521	2
β-strand	527-529	3	10
β-strand	549-551	3	10

Chain B: 21 helices, 33 β-strands

Element	Residues	Length	Sheet
β-strand	9	1	11
β-strand	12-13	2	12
α-helix	15-22	8
β-strand	23	1	13
β-strand	28-32	5	13
β-strand	35-37	3	12
β-strand	39-40	2	11
β-strand	51-55	5	13
β-strand	71-72	2	14
α-helix	73	1
β-strand	79-80	2	14
α-helix	82-84	3
β-strand	113	1	15
α-helix	114-115	2
α-helix	118-122	5
β-strand	123-125	3	16
β-strand	132-135	4	16
β-strand	137	1	17
β-strand	147-151	5	15
β-strand	154-158	5	15
β-strand	162-167	6	16
β-strand	175-180	6	18
α-helix	183-186	4
β-strand	201	1	19
β-strand	205	1	19
β-strand	210-211	2	16
α-helix	222-229	8
β-strand	236-243	8	18
β-strand	245-252	8	16
β-strand	259	1	17
α-helix	261-267	7
α-helix	276-286	11
β-strand	289-298	10	16
β-strand	301-307	7	18
α-helix	308-311	4
α-helix	318-324	7
α-helix	355-358	4
β-strand	366-372	7	18
α-helix	381-385	5
α-helix	395-403	9
β-strand	407-415	9	16
α-helix	416-419	4
α-helix	428-445	18
α-helix	448-450	3
α-helix	452-453	2
β-strand	459-463	5	11
β-strand	466-470	5	11
β-strand	475-476	2	20
α-helix	478-480	3
β-strand	482-483	2	20
α-helix	488-492	5
α-helix	496-500	5
β-strand	506-509	4	21
β-strand	531-534	4	21

Chain C: 8 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	17-19	3
β-strand	29-37	9	22
α-helix	41-44	4
α-helix	46-49	4
α-helix	50-52	3
β-strand	54-60	7	22
β-strand	63-72	10	22
β-strand	75-85	11	22
β-strand	91-94	4	22
β-strand	103-110	8	22
β-strand	115-122	8	22
β-strand	125-132	8	22
α-helix	137-138	2
α-helix	139-149	11
α-helix	156-158	3
β-strand	159-161	3	22
α-helix	162-163	2
β-strand	172	1	23
β-strand	175	1	23
β-strand	176-177	2	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement component C8 alpha chain	A	protein	554	Homo sapiens	P07357 (AlphaFold model)
Complement component C8 beta chain	B	protein	537	Homo sapiens	P07358 (AlphaFold model)
Complement component C8 gamma chain	C	protein	182	Homo sapiens	P07360 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3OJY_1 Complement component C8 alpha chain (chains A)
AATPAAVTCQLSNWSEWTDCFPCQDKKYRHRSLLQPNKFGGTICSGDIWDQASCSSSTTC
VRQAQCGQDFQCKETGRCLKRHLVCNGDQDCLDGSDEDDCEDVRAIDEDCSQYEPIPGSQ
KAALGYNILTQEDAQSVYDASYYGGQCETVYNGEWRELRYDSTCERLYYGDDEKYFRKPY
NFLKYHFEALADTGISSEFYDNANDLLSKVKKDKSDSFGVTIGIGPAGSPLLVGVGVSHS
QDTSFLNELNKYNEKKFIFTRIFTKVQTAHFKMRKDDIMLDEGMLQSLMELPDQYNYGMY
AKFINDYGTHYITSGSMGGIYEYILVIDKAKMESLGITSRDITTCFGGSLGIQYEDKINV
GGGLSGDHCKKFGGGKTERARKAMAVEDIISRVRGGSSGWSGGLAQNRSTITYRSWGRSL
KYNPVVIDFEMQPIHEVLRHTSLGPLEAKRQNLRRALDQYLMEFNACRCGPCFNNGVPIL
EGTSCRCQCRLGSLGAACEQTQTEGAKADGSWSCWSSWSVCRAGIQERRRECDNPAPQNG
GASCPGRKVQTQAC

Sequence of entity 2 (B), FASTA

>3OJY_2 Complement component C8 beta chain (chains B)
SVDVTLMPIDCELSSWSSWTTCDPCQKKRYRYAYLLQPSQFHGEPCNFSDKEVEDCVTNR
PCRSQVRCEGFVCAQTGRCVNRRLLCNGDNDCGDQSDEANCRRIYKKCQHEMDQYWGIGS
LASGINLFTNSFEGPVLDHRYYAGGCSPHYILNTRFRKPYNVESYTPQTQGKYEFILKEY
ESYSDFERNVTEKMASKSGFSFGFKIPGIFELGISSQSDRGKHYIRRTKRFSHTKSVFLH
ARSDLEVAHYKLKPRSLMLHYEFLQRVKRLPLEYSYGEYRDLFRDFGTHYITEAVLGGIY
EYTLVMNKEAMERGDYTLNNVHACAKNDFKIGGAIEEVYVSLGVSVGKCRGILNEIKDRN
KRDTMVEDLVVLVRGGASEHITTLAYQELPTADLMQEWGDAVQYNPAIIKVKVEPLYELV
TATDFAYSSTVRQNMKQALEEFQKEVSSCHCAPCQGNGVPVLKGSRCDCICPVGSQGLAC
EVSYRKNTPIDGKWNCWSNWSSCSGRRKTRQRQCNNPPPQNGGSPCSGPASETLDCS

Sequence of entity 3 (C), FASTA

>3OJY_3 Complement component C8 gamma chain (chains C)
QKPQRPRRPASPISTIQPKANFDAQQFAGTWLLVAVGSACRFLQEQGHRAEATTLHVAPQ
GTAMAVSTFRKLDGICWQVRQLYGDTGVLGRFLLQARDARGAVHVVVAETDYQSFAVLYL
ERAGQLSVKLYARSLPVSDSVLSGFEQRVQEAHLTEDQIFYFPKYGFCEAADQFHVLDEV
RR

Ligands and cofactors

ID	Name	Formula	Copies
BMA	beta-D-mannopyranose	C6 H12 O6	8
CA	Calcium ion	Ca	2

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…
2RD7 2.15 Å, Human Complement Membrane Attack Proteins Share a Common Fold with Bacterial Cytolysins
2QQH 2.5 Å, Structure of C8a-MACPF reveals mechanism of membrane attack in complement immune defense
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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