Crystal structure of the Helicobacter pylori CagA oncoprotein. Determined by X-ray diffraction at 3.3 Å resolution. Released 25 Jul 2012.
Explore 4DVY in 3D Show helices and sheets RCSB PDB PDBe
4DVY contains 27 α-helices and 13 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 25-44 | 20 | |
| α-helix | 49-79 | 31 | |
| α-helix | 81-83 | 3 | |
| α-helix | 84-101 | 18 | |
| α-helix | 107-112 | 6 | |
| α-helix | 122-131 | 10 | |
| α-helix | 135-137 | 3 | |
| α-helix | 140-146 | 7 | |
| α-helix | 158-183 | 26 | |
| α-helix | 185-190 | 6 | |
| α-helix | 192-203 | 12 | |
| α-helix | 212-218 | 7 | |
| β-strand | 309-313 | 5 | 1 |
| β-strand | 320-325 | 6 | 1 |
| β-strand | 336-342 | 7 | 1 |
| β-strand | 351-358 | 8 | 1 |
| β-strand | 363-367 | 5 | 1 |
| α-helix | 376-379 | 4 | |
| β-strand | 381-383 | 3 | 2 |
| β-strand | 390-392 | 3 | 2 |
| α-helix | 393-394 | 2 | |
| α-helix | 395-410 | 16 | |
| α-helix | 420-425 | 6 | |
| α-helix | 427-435 | 9 | |
| α-helix | 438-446 | 9 | |
| β-strand | 448-452 | 5 | 1 |
| α-helix | 453-455 | 3 | |
| β-strand | 460-467 | 8 | 1 |
| β-strand | 471-477 | 7 | 1 |
| β-strand | 493-495 | 3 | 1 |
| β-strand | 503-507 | 5 | 1 |
| β-strand | 539-543 | 5 | 1 |
| α-helix | 556-567 | 12 | |
| α-helix | 572-606 | 35 | |
| α-helix | 610-639 | 30 | |
| α-helix | 649-708 | 60 | |
| α-helix | 723-733 | 11 | |
| α-helix | 738-753 | 16 | |
| α-helix | 763-802 | 40 | |
| α-helix | 806-821 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cytotoxicity-associated immunodominant antigen | P | protein | 876 | Helicobacter pylori | P55980 (AlphaFold model) |
>4DVY_1 Cytotoxicity-associated immunodominant antigen (chains P) MTNETIDQTRTPDQTQSQTAFDPQQFINNLQVAFIKVDNVVASFDPDQKPIVDKNDRDNR QAFDGISQLREEYSNKAIKNPTKKNQYFSDFIDKSNDLINKDNLIDVESSTKSFQKFGDQ RYQIFTSWVSMQKDPSKINTRSIRNFMENIIQPPIPDDKEKAEFLKSAKQSFAGIIIGNQ IRTDQKFMGVFDESLKERQEAEKNGGPTGGDWLDIFLSFIFNKKQSSDVKEAINQEPVPH VQPDIATTTTDIQGLPPEARDLLDERGNFSKFTMGDMEMLDVEGVADIDPNYKFNQLLIH NNALSSVLMGSHNGIEPEKVSLLYAGNGGFGDKHDWNATVGYKDQQGNNVATLINVHMKN GSGLVIAGGEKGINNPSFYLYKEDQLTGSQRALSQEEIRNKVDFMEFLAQNNTKLDNLSE KEKEKFQNEIEDFQKDSKAYLDALGNDRIAFVSKKDTKHSALITEFNNGDLSYTLKDYGK KADKALDREKNVTLQGSLKHDGVMFVDYSNFKYTNASKNPNKGVGATNGVSHLEAGFNKV AVFNLPDLNNLAITSFVRRNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKALNFNKAV AEAKSTGNYDEVKKAQKDLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQKDEI FALINKEANRDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKA EETLKALKGSVKDLGINPEWISKVENLNAALNEFKNGKNKDFSKVTQAKSDLENSVKDVI INQKVTDKVDNLNQAVSVAKAMGDFSRVEQVLADLKNFSKEQLAQQAQKNEDFNTGKNSE LYQSVKNSVNKTLVGNGLSGIEATALAKNFSDIKKE
Tertiary Structure-Function Analysis Reveals the Pathogenic Signaling Potentiation Mechanism of Helicobacter pylori Oncogenic Effector CagA. Hayashi, T., Senda, M., Morohashi, H. et al. Cell Host Microbe (2012) 12:20-33. DOI 10.1016/j.chom.2012.05.010 · PubMed
Other PDB entries of the same protein (UniProt P55980 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 4DVY directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.