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

ElementResiduesLengthSheet
α-helix5-1814
α-helix21-3212
α-helix40-6728
α-helix76-10227
α-helix103-1075
α-helix108-1103
α-helix114-13421
α-helix138-16124
α-helix167-18216
α-helix187-20317
α-helix205-2073
α-helix213-23018
Chain B: 12 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix5-1814
α-helix21-3212
α-helix40-6930
α-helix79-10224
α-helix103-1075
α-helix108-1103
α-helix114-13421
α-helix138-16124
α-helix167-18216
α-helix187-20317
α-helix205-2073
α-helix213-23220
Chain C: 13 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix6-1712
α-helix21-3212
α-helix37-393
α-helix40-6829
α-helix79-10224
α-helix103-1075
α-helix108-1103
α-helix114-13421
α-helix138-16124
α-helix167-18216
α-helix187-20317
α-helix205-2073
α-helix213-23321
Chain D: 13 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix5-1814
α-helix21-3212
α-helix36-394
α-helix40-7031
α-helix79-10224
α-helix103-1075
α-helix108-1103
α-helix114-13421
α-helix138-16124
α-helix167-18216
α-helix187-20317
α-helix205-2073
α-helix213-23321
Chain E: 11 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix235-2428
α-helix247-2504
α-helix263-2719
α-helix272-2765
α-helix277-28610
α-helix289-2913
α-helix292-30817
β-strand315-32171
α-helix326-3294
α-helix3311
β-strand335-33731
β-strand342-34432
β-strand34511
β-strand358-36471
β-strand368-36922
β-strand382-38432
β-strand389-39681
β-strand403-40971
α-helix410-4123
α-helix422-4254
Chain F: 12 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix235-24410
α-helix247-2504
α-helix253-2553
α-helix263-2719
α-helix272-2765
α-helix277-28610
α-helix292-30716
α-helix3141
β-strand315-31953
α-helix326-3294
α-helix3311
β-strand335-33733
β-strand342-34543
β-strand358-36473
β-strand368-36923
β-strand381-38443
β-strand389-39793
β-strand403-40973
α-helix410-4123
α-helix422-4254
Chain G: 11 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix235-24410
α-helix247-2504
α-helix263-2719
α-helix272-2765
α-helix277-28610
α-helix292-30413
β-strand315-32174
α-helix326-3294
α-helix3311
β-strand335-33734
β-strand342-34544
β-strand358-36474
β-strand368-36924
β-strand381-38444
α-helix3851
β-strand389-39684
β-strand403-40974
α-helix410-4123
α-helix422-4254
Chain H: 13 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix235-24410
α-helix247-2504
α-helix263-2719
α-helix272-2765
α-helix277-2859
α-helix289-2913
α-helix294-30613
β-strand315-32175
α-helix326-3283
α-helix3311
β-strand335-33735
β-strand342-34545
α-helix350-3523
β-strand358-36475
β-strand368-36925
β-strand381-38445
α-helix3851
β-strand389-39795
β-strand403-40975
α-helix410-4123
α-helix422-4254

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
14-3-3 protein beta/alphaA, B, C, Dprotein248Homo sapiensP31946 (AlphaFold model)
Exoenzyme SE, F, G, Hprotein244Pseudomonas aeruginosaQ93SQ1 (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:

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