3OHX: Complement C3
Molecular Basis for Complement Recognition and Inhibition Determined by Crystallographic Studies of the Staphylococcal Complement Inhibitor (SCIN) Bound to C3c and C3b. Determined by X-ray diffraction at 3.5 Å resolution. Released 1 Sept 2010.
- Method
- X-ray diffraction
- Resolution
- 3.5 Å
- Organisms
- Homo sapiens, Staphylococcus aureus
- Chains
- 8
- Atoms
- 19,119
- Mol. weight
- 289.68 kDa
- Ligands
- NAG
- Released
- 1 Sept 2010
Explore 3OHX in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3OHX contains 50 α-helices and 196 β-strands across 8 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 and D: 11 helices, 59 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-8 | 6 | 1 |
| β-strand | 11-13 | 3 | 2 |
| β-strand | 17-25 | 9 | 1 |
| β-strand | 31-39 | 9 | 2 |
| β-strand | 47 | 1 | 2 |
| β-strand | 51-54 | 4 | 2 |
| β-strand | 61-67 | 7 | 1 |
| β-strand | 83-90 | 8 | 2 |
| β-strand | 93-102 | 10 | 2 |
| β-strand | 106-112 | 7 | 3 |
| β-strand | 116-117 | 2 | 4 |
| β-strand | 123-124 | 2 | 5 |
| β-strand | 125-131 | 7 | 3 |
| β-strand | 136 | 1 | 3 |
| β-strand | 140-146 | 7 | 4 |
| β-strand | 152-159 | 8 | 4 |
| β-strand | 166-167 | 2 | 3 |
| β-strand | 170-171 | 2 | 5 |
| β-strand | 180-188 | 9 | 4 |
| β-strand | 191-202 | 12 | 4 |
| α-helix | 206-208 | 3 | |
| β-strand | 210-216 | 7 | 6 |
| β-strand | 221-222 | 2 | 7 |
| β-strand | 229-237 | 9 | 6 |
| β-strand | 242 | 1 | 6 |
| β-strand | 245-255 | 11 | 8 |
| β-strand | 258-261 | 4 | 8 |
| α-helix | 263-265 | 3 | |
| β-strand | 267-271 | 5 | 8 |
| β-strand | 272 | 1 | 6 |
| β-strand | 275-280 | 6 | 6 |
| α-helix | 282-287 | 6 | |
| α-helix | 294-297 | 4 | |
| β-strand | 301-310 | 10 | 8 |
| β-strand | 316-325 | 10 | 8 |
| β-strand | 326-327 | 2 | 7 |
| β-strand | 332-334 | 3 | 9 |
| β-strand | 341-342 | 2 | 10 |
| β-strand | 347-355 | 9 | 9 |
| β-strand | 361 | 1 | 9 |
| β-strand | 367-369 | 3 | 11 |
| β-strand | 377 | 1 | 11 |
| β-strand | 380 | 1 | 9 |
| β-strand | 384-390 | 7 | 9 |
| α-helix | 391-392 | 2 | |
| β-strand | 398-404 | 7 | 11 |
| β-strand | 416-421 | 6 | 11 |
| β-strand | 422-423 | 2 | 10 |
| α-helix | 424 | 1 | |
| β-strand | 433-438 | 6 | 12 |
| β-strand | 443 | 1 | 13 |
| β-strand | 445 | 1 | 14 |
| β-strand | 447 | 1 | 14 |
| β-strand | 448-456 | 9 | 12 |
| α-helix | 459-462 | 4 | |
| β-strand | 467-474 | 8 | 15 |
| β-strand | 477-485 | 9 | 15 |
| β-strand | 492-498 | 7 | 12 |
| α-helix | 501-503 | 3 | |
| β-strand | 506-517 | 12 | 15 |
| β-strand | 521-532 | 12 | 15 |
| β-strand | 533 | 1 | 13 |
| β-strand | 541-545 | 5 | 16 |
| β-strand | 558-566 | 9 | 16 |
| β-strand | 570-577 | 8 | 17 |
| α-helix | 580-582 | 3 | |
| α-helix | 591-599 | 9 | |
| β-strand | 608 | 1 | 15 |
| α-helix | 613-619 | 7 | |
| β-strand | 623-626 | 4 | 1 |
Chains B and E: 2 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 736-738 | 3 | |
| β-strand | 742 | 1 | 18 |
| β-strand | 748-749 | 2 | 17 |
| β-strand | 753-755 | 3 | 17 |
| β-strand | 764-772 | 9 | 16 |
| β-strand | 779-788 | 10 | 17 |
| β-strand | 792-795 | 4 | 17 |
| α-helix | 796-798 | 3 | |
| β-strand | 799-802 | 4 | 17 |
| β-strand | 807-812 | 6 | 19 |
| β-strand | 816-818 | 3 | 18 |
| β-strand | 823-831 | 9 | 19 |
| β-strand | 838-844 | 7 | 18 |
| β-strand | 850 | 1 | 20 |
| β-strand | 860-866 | 7 | 18 |
| β-strand | 870-878 | 9 | 19 |
| β-strand | 880 | 1 | 20 |
| β-strand | 884-894 | 11 | 18 |
| β-strand | 900-910 | 11 | 18 |
Chain C: 9 helices, 23 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1339-1347 | 9 | 21 |
| β-strand | 1362-1370 | 9 | 21 |
| α-helix | 1375 | 1 | |
| β-strand | 1376 | 1 | 22 |
| β-strand | 1379-1384 | 6 | 23 |
| β-strand | 1389-1391 | 3 | 21 |
| α-helix | 1393-1401 | 9 | |
| β-strand | 1405-1406 | 2 | 23 |
| α-helix | 1409-1413 | 5 | |
| α-helix | 1416-1418 | 3 | |
| β-strand | 1421-1426 | 6 | 23 |
| β-strand | 1429 | 1 | 22 |
| β-strand | 1435-1443 | 9 | 21 |
| α-helix | 1451-1452 | 2 | |
| β-strand | 1453-1459 | 7 | 23 |
| β-strand | 1467-1471 | 5 | 23 |
| β-strand | 1482-1485 | 4 | 24 |
| β-strand | 1488-1491 | 4 | 24 |
| α-helix | 1509-1514 | 6 | |
| β-strand | 1522 | 1 | 25 |
| β-strand | 1523-1524 | 2 | 26 |
| β-strand | 1526-1527 | 2 | 27 |
| β-strand | 1531 | 1 | 27 |
| β-strand | 1536-1542 | 7 | 27 |
| β-strand | 1548 | 1 | 25 |
| β-strand | 1559-1565 | 7 | 27 |
| α-helix | 1566-1568 | 3 | |
| β-strand | 1581-1582 | 2 | 26 |
| β-strand | 1589-1590 | 2 | 27 |
| β-strand | 1597-1599 | 3 | 27 |
| α-helix | 1623-1625 | 3 | |
| α-helix | 1627-1635 | 9 | |
Chain F: 7 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1339-1347 | 9 | 33 |
| β-strand | 1362-1370 | 9 | 33 |
| α-helix | 1375 | 1 | |
| β-strand | 1376 | 1 | 34 |
| β-strand | 1379-1384 | 6 | 35 |
| β-strand | 1389-1391 | 3 | 33 |
| α-helix | 1393-1401 | 9 | |
| β-strand | 1405-1406 | 2 | 35 |
| α-helix | 1409-1412 | 4 | |
| α-helix | 1416-1418 | 3 | |
| β-strand | 1421-1426 | 6 | 35 |
| β-strand | 1429 | 1 | 34 |
| β-strand | 1435-1443 | 9 | 33 |
| α-helix | 1451-1452 | 2 | |
| β-strand | 1453-1459 | 7 | 35 |
| β-strand | 1467-1471 | 5 | 35 |
| β-strand | 1482-1485 | 4 | 36 |
| β-strand | 1488-1491 | 4 | 36 |
| β-strand | 1522-1526 | 5 | 37 |
| β-strand | 1527-1530 | 4 | 38 |
| β-strand | 1537-1541 | 5 | 38 |
| β-strand | 1548 | 1 | 37 |
| α-helix | 1549-1550 | 2 | |
| β-strand | 1560-1564 | 5 | 38 |
| β-strand | 1579-1583 | 5 | 37 |
| β-strand | 1599 | 1 | 38 |
| β-strand | 1605-1606 | 2 | 37 |
| α-helix | 1621-1634 | 14 | |
Chains M and P: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-24 | 18 | |
| α-helix | 26-32 | 7 | |
| α-helix | 38-57 | 20 | |
| α-helix | 60-82 | 23 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Complement C3 | A, D | protein | 645 | Homo sapiens | P01024 (AlphaFold model) |
| Complement C3 | B, E | protein | 206 | Homo sapiens | P01024 (AlphaFold model) |
| Complement C3 | C, F | protein | 343 | Homo sapiens | P01024 (AlphaFold model) |
| Staphylococcal complement inhibitor | M, P | protein | 88 | Staphylococcus aureus | Q931M7 (AlphaFold model) |
Sequence of entity 1 (A, D), FASTA
>3OHX_1 Complement C3 (chains A, D)
SPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDFPGKKLVLSSEKTVLTPATNH
MGNVTFTIPANREFKSEKGRNKFVTVQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPG
STVLYRIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSSQNQLGVLPLSWDIPELVNMG
QWKIRAYYENSPQQVFSTEFEVKEYVLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYG
KKVEGTAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVLSRKVLLDGVQNPRAEDLVGK
SLYVSATVILHSGSDMVQAERSGIPIVTSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGS
PAYRVPVAVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSITVRTKKQELSEAEQATRTMQ
ALPYSTVGNSNNYLHLSVLRTELRPGETLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLK
AGRQVREPGQDLVVLPLSITTDFIPSFRLVAYYTLIGASGQREVVADSVWVDVKDSCVGS
LVVKSGQSEDRQPVPGQQMTLKIEGDHGARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEK
ADIGCTPGSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQCPQPAA
Sequence of entity 2 (B, E), FASTA
>3OHX_2 Complement C3 (chains B, E)
SNLDEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKLMNIFLKDSITTWEILAVS
MSDKKGICVADPFEVTVMQDFFIDLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLH
NPAFCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEVEVKAAVYHHFISDGVRKS
LKVVPEGIRMNKTVAVRTLDPERLGR
Sequence of entity 3 (C, F), FASTA
>3OHX_3 Complement C3 (chains C, F)
SEETKENEGFTVTAEGKGQGTLSVVTMYHAKAKDQLTCNKFDLKVTIKPAPETEKRPQDA
KNTMILEICTRYRGDQDATMSILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSD
RNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVYAYYNLEESCTRFYHPEKEDG
KLNKLCRDELCRCAEENCFIQKSDDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDE
YIMAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKHYLMWGLSSDFWGEKPNLSY
IIGKDTWVEHWPEEDECQDEENQKQCQDLGAFTESMVVFGCPN
Sequence of entity 4 (M, P), FASTA
>3OHX_4 Staphylococcal complement inhibitor (chains M, P)
GTSSTSLPTSNEYQNEKLANELKSLLDELNVNELATGSLNTYYKRTIKISGQKAMYALKS
KDFKKMSEAKYQLQKIYNEIDEALKSKY
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
Primary citation
Molecular Basis for Complement Recognition and Inhibition Determined by Crystallographic Studies of the Staphylococcal Complement Inhibitor (SCIN) Bound to C3c and C3b. Garcia, B.L., Ramyar, K.X., Tzekou, A. et al. J Mol Biol (2010) 402:17-29. DOI 10.1016/j.jmb.2010.07.029 · PubMed
Other PDB entries of the same protein (UniProt P01024 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2WY7 1.7 Å, Staphylococcus aureus complement subversion protein Sbi-IV in complex with complement…
- 2WY8 1.7 Å, Staphylococcus aureus complement subversion protein Sbi-IV in complex with complement…
- 7UE9 1.75 Å, Structure of anti-C3d Fab(3d8b) in complex with C3d
- 1C3D 1.8 Å, X-ray crystal structure of C3D: a C3 fragment and ligand for complement receptor 2
- 6RMT 2.0 Å, Crystal structure of disulphide-linked human C3d dimer
- 7BAG 2.0 Å, C3b in complex with CP40
- 1GHQ 2.04 Å, CR2-C3D complex structure
- 3D5R 2.1 Å, Crystal Structure of Efb-C (N138A) / C3d Complex
- 3OXU 2.1 Å, Complement components factor H CCP19-20 and C3d in complex
- 4I6O 2.14 Å, Crystal structure of chemically synthesized human anaphylatoxin C3a
- 4ONT 2.15 Å, Ternary host recognition complex of complement factor H, C3d, and sialic acid
- 2GOX 2.2 Å, Crystal structure of Efb-C / C3d Complex
Browse structure collections
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