4FN2: PDB entry 4FN2

Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase with surface mutation D44G from Burkholderia pseudomallei complexed with CJ37. Determined by X-ray diffraction at 1.95 Å resolution. Released 1 Aug 2012.

Method
X-ray diffraction
Resolution
1.95 Å
Organisms
Saccharomyces cerevisiae, Burkholderia pseudomallei
Chains
2
Atoms
3,183
Mol. weight
46.51 kDa
Ligands
854
Released
1 Aug 2012

Explore 4FN2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4FN2 contains 15 α-helices and 32 β-strands across 2 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: 7 helices, 16 β-strands

ElementResiduesLengthSheet
β-strand-75--6971
β-strand-64--5871
α-helix-52--4310
α-helix-38--363
β-strand-35--3151
β-strand-28--2721
α-helix-261
β-strand-11--571
β-strand3-532
β-strand11-1662
β-strand1913
α-helix22-232
β-strand28-37102
β-strand42-4542
β-strand53-5642
α-helix64-696
β-strand7513
β-strand78-8362
α-helix85-873
β-strand9414
β-strand9814
α-helix991
β-strand104-11292
Chain B: 8 helices, 16 β-strands
ElementResiduesLengthSheet
β-strand-74--6965
β-strand-64--5965
α-helix-52--4310
α-helix-38--363
β-strand-35--3155
β-strand-28--2725
α-helix-261
α-helix-19--173
β-strand-10--565
β-strand4-526
β-strand11-1666
α-helix211
β-strand2217
α-helix231
β-strand28-37106
β-strand42-4546
β-strand53-5646
α-helix64-696
β-strand7417
β-strand78-8366
α-helix85-873
β-strand9418
β-strand9818
β-strand104-11296

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin-like protein SMT3, Peptidyl-prolyl cis-trans isomeraseA, Bprotein209Saccharomyces cerevisiae, Burkholderia pseudomalleiQ12306 (AlphaFold model), Q3JK38 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4FN2_1 Ubiquitin-like protein SMT3, Peptidyl-prolyl cis-trans isomerase (chains A, B)
MGHHHHHHSGEVKPEVKPETHINLKVSDGSSEIFFKIKKTTPLRRLMEAFAKRQGKEMDS
LRFLYDGIRIQADQTPEDLDMEDNDIIEAHREQIGGSTVVTTESGLKYEDLTEGSGAEAR
AGQTVSVHYTGWLTDGQKFGSSKDRNDPFAFVLGGGMVIKGWDEGVQGMKVGGVRRLTIP
PQLGYGARGAGGVIPPNATLVFEVELLDV

Ligands and cofactors

IDNameFormulaCopies
854ethyl (2S)-1-(benzylsulfonyl)piperidine-2-carboxylateC15 H21 N O4 S2

Primary citation

A structural biology approach enables the development of antimicrobials targeting bacterial immunophilins. Begley, D.W., Fox, D., Jenner, D. et al. Antimicrob Agents Chemother (2014) 58:1458-1467. DOI 10.1128/AAC.01875-13 · PubMed

Other PDB entries of the same protein (UniProt Q12306 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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