6GN0: Exoenzyme S from Pseudomonas aeruginosa
Exoenzyme S from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta, tetrameric crystal form. Determined by X-ray diffraction at 3.24 Å resolution. Released 26 Sept 2018.
- Method
- X-ray diffraction
- Resolution
- 3.24 Å
- Organisms
- Homo sapiens, Pseudomonas aeruginosa
- Chains
- 8
- Atoms
- 13,303
- Mol. weight
- 219.12 kDa
- Released
- 26 Sept 2018
Explore 6GN0 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6GN0 contains 97 α-helices and 33 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.
Chain A: 12 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-18 | 14 | |
| α-helix | 21-32 | 12 | |
| α-helix | 40-67 | 28 | |
| α-helix | 76-102 | 27 | |
| α-helix | 103-107 | 5 | |
| α-helix | 108-110 | 3 | |
| α-helix | 114-134 | 21 | |
| α-helix | 138-161 | 24 | |
| α-helix | 167-182 | 16 | |
| α-helix | 187-203 | 17 | |
| α-helix | 205-207 | 3 | |
| α-helix | 213-230 | 18 | |
Chain B: 12 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-18 | 14 | |
| α-helix | 21-32 | 12 | |
| α-helix | 40-69 | 30 | |
| α-helix | 79-102 | 24 | |
| α-helix | 103-107 | 5 | |
| α-helix | 108-110 | 3 | |
| α-helix | 114-134 | 21 | |
| α-helix | 138-161 | 24 | |
| α-helix | 167-182 | 16 | |
| α-helix | 187-203 | 17 | |
| α-helix | 205-207 | 3 | |
| α-helix | 213-232 | 20 | |
Chain C: 13 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-17 | 12 | |
| α-helix | 21-32 | 12 | |
| α-helix | 37-39 | 3 | |
| α-helix | 40-68 | 29 | |
| α-helix | 79-102 | 24 | |
| α-helix | 103-107 | 5 | |
| α-helix | 108-110 | 3 | |
| α-helix | 114-134 | 21 | |
| α-helix | 138-161 | 24 | |
| α-helix | 167-182 | 16 | |
| α-helix | 187-203 | 17 | |
| α-helix | 205-207 | 3 | |
| α-helix | 213-233 | 21 | |
Chain D: 13 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-18 | 14 | |
| α-helix | 21-32 | 12 | |
| α-helix | 36-39 | 4 | |
| α-helix | 40-70 | 31 | |
| α-helix | 79-102 | 24 | |
| α-helix | 103-107 | 5 | |
| α-helix | 108-110 | 3 | |
| α-helix | 114-134 | 21 | |
| α-helix | 138-161 | 24 | |
| α-helix | 167-182 | 16 | |
| α-helix | 187-203 | 17 | |
| α-helix | 205-207 | 3 | |
| α-helix | 213-233 | 21 | |
Chain E: 11 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 235-242 | 8 | |
| α-helix | 247-250 | 4 | |
| α-helix | 263-271 | 9 | |
| α-helix | 272-276 | 5 | |
| α-helix | 277-286 | 10 | |
| α-helix | 289-291 | 3 | |
| α-helix | 292-308 | 17 | |
| β-strand | 315-321 | 7 | 1 |
| α-helix | 326-329 | 4 | |
| α-helix | 331 | 1 | |
| β-strand | 335-337 | 3 | 1 |
| β-strand | 342-344 | 3 | 2 |
| β-strand | 345 | 1 | 1 |
| β-strand | 358-364 | 7 | 1 |
| β-strand | 368-369 | 2 | 2 |
| β-strand | 382-384 | 3 | 2 |
| β-strand | 389-396 | 8 | 1 |
| β-strand | 403-409 | 7 | 1 |
| α-helix | 410-412 | 3 | |
| α-helix | 422-425 | 4 | |
Chain F: 12 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 235-244 | 10 | |
| α-helix | 247-250 | 4 | |
| α-helix | 253-255 | 3 | |
| α-helix | 263-271 | 9 | |
| α-helix | 272-276 | 5 | |
| α-helix | 277-286 | 10 | |
| α-helix | 292-307 | 16 | |
| α-helix | 314 | 1 | |
| β-strand | 315-319 | 5 | 3 |
| α-helix | 326-329 | 4 | |
| α-helix | 331 | 1 | |
| β-strand | 335-337 | 3 | 3 |
| β-strand | 342-345 | 4 | 3 |
| β-strand | 358-364 | 7 | 3 |
| β-strand | 368-369 | 2 | 3 |
| β-strand | 381-384 | 4 | 3 |
| β-strand | 389-397 | 9 | 3 |
| β-strand | 403-409 | 7 | 3 |
| α-helix | 410-412 | 3 | |
| α-helix | 422-425 | 4 | |
Chain G: 11 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 235-244 | 10 | |
| α-helix | 247-250 | 4 | |
| α-helix | 263-271 | 9 | |
| α-helix | 272-276 | 5 | |
| α-helix | 277-286 | 10 | |
| α-helix | 292-304 | 13 | |
| β-strand | 315-321 | 7 | 4 |
| α-helix | 326-329 | 4 | |
| α-helix | 331 | 1 | |
| β-strand | 335-337 | 3 | 4 |
| β-strand | 342-345 | 4 | 4 |
| β-strand | 358-364 | 7 | 4 |
| β-strand | 368-369 | 2 | 4 |
| β-strand | 381-384 | 4 | 4 |
| α-helix | 385 | 1 | |
| β-strand | 389-396 | 8 | 4 |
| β-strand | 403-409 | 7 | 4 |
| α-helix | 410-412 | 3 | |
| α-helix | 422-425 | 4 | |
Chain H: 13 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 235-244 | 10 | |
| α-helix | 247-250 | 4 | |
| α-helix | 263-271 | 9 | |
| α-helix | 272-276 | 5 | |
| α-helix | 277-285 | 9 | |
| α-helix | 289-291 | 3 | |
| α-helix | 294-306 | 13 | |
| β-strand | 315-321 | 7 | 5 |
| α-helix | 326-328 | 3 | |
| α-helix | 331 | 1 | |
| β-strand | 335-337 | 3 | 5 |
| β-strand | 342-345 | 4 | 5 |
| α-helix | 350-352 | 3 | |
| β-strand | 358-364 | 7 | 5 |
| β-strand | 368-369 | 2 | 5 |
| β-strand | 381-384 | 4 | 5 |
| α-helix | 385 | 1 | |
| β-strand | 389-397 | 9 | 5 |
| β-strand | 403-409 | 7 | 5 |
| α-helix | 410-412 | 3 | |
| α-helix | 422-425 | 4 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| 14-3-3 protein beta/alpha | A, B, C, D | protein | 248 | Homo sapiens | P31946 (AlphaFold model) |
| Exoenzyme S | E, F, G, H | protein | 244 | Pseudomonas aeruginosa | Q93SQ1 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D), FASTA
>6GN0_1 14-3-3 protein beta/alpha (chains A, B, C, D)
MTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSS
WRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLELLDKYLIPNATQPESKVFY
LKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFY
YEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGDEGE
NLYFQSLE
Sequence of entity 2 (E, F, G, H), FASTA
>6GN0_2 Exoenzyme S (chains E, F, G, H)
MGSSHHHHHHSQDPNSENLYFQGADKALADGLVKRFGADAEKYLGRQPGGIHSDAEVMAL
GLYTGIHYADLNRALRQGQELDAGQKLIDQGMSAAFEKSGQAEQVVKTFRGTRGGDAFNA
VEEGKVGHDDGYLSTSLNPGVARSFGQGTISTVFGRSGIDVSGISNYKNAKAILYNKETD
MRVLLSASDEQGVTRRVLEEAALGELSGHSQGLLDALDLASKPEPSGEVQEQDVRLRMRG
LDLA
Primary citation
14-3-3 proteins activate Pseudomonas exotoxins-S and -T by chaperoning a hydrophobic surface. Karlberg, T., Hornyak, P., Pinto, A.F. et al. Nat Commun (2018) 9:3785-3785. DOI 10.1038/s41467-018-06194-1 · PubMed
Other PDB entries of the same protein (UniProt P31946 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8EQ8 1.5 Å, The crystal structure of 14-3-3 Beta containing 3-nitrotyrosine at position Y130
- 5N10 1.6 Å, Cucurbit[8]uril and 14-3-3 based binary bivalent supramolecular-protein assembly platform
- 6HEP 1.86 Å, Crystal structure of human 14-3-3 beta in complex with CFTR R-domain peptide pS753-pS768
- 8EQH 1.9 Å, The crystal structure of 14-3-3 Beta containing 3-nitrotyrosine at position Y213
- 6A5Q 2.0 Å, Structure of 14-3-3 beta in complex with TFEB 14-3-3 binding motif
- 6YGJ 2.07 Å, small-molecule stabilizer of 14-3-3 and the Carbohydrate Response Element Binding…
- 4DNK 2.2 Å, Crystal structure of a tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation…
- 6GN8 2.34 Å, Exoenzyme S from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta,…
- 2BQ0 2.5 Å, 14-3-3 Protein Beta (Human)
- 6GNK 2.55 Å, Exoenzyme S from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta,…
- 9GCP 2.59 Å, ChREBP/14-3-3 complex stabilized by AMP
- 2C23 2.65 Å, 14-3-3 Protein Beta (Human) in complex with exoenzyme S peptide
Browse structure collections
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