5LNC: PDB entry 5LNC

Structure of SPX domain of the yeast inorganic polyphophate polymerase Vtc4 crystallized by carrier-driven crystallization in fusion with the macro domain of human histone macroH2A1.1. Determined by X-ray diffraction at 3.29 Å resolution. Released 9 Nov 2016.

Method
X-ray diffraction
Resolution
3.29 Å
Organisms
Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Homo sapiens
Chains
2
Atoms
4,673
Mol. weight
84.47 kDa
Released
9 Nov 2016

Explore 5LNC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5LNC contains 28 α-helices and 16 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: 14 helices, 9 β-strands

ElementResiduesLengthSheet
α-helix4-85
α-helix13-153
α-helix22-3514
α-helix42-8746
β-strand8911
β-strand9111
α-helix95-13743
α-helix143-1519
α-helix160-17819
β-strand188-19142
β-strand197-20152
α-helix205-2073
β-strand212-21762
α-helix225-25026
α-helix253-2542
β-strand258-26252
β-strand270-27562
α-helix276-2783
α-helix284-30118
β-strand306-30942
α-helix321-33818
β-strand346-35052
α-helix354-36512
Chain B: 14 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix4-85
α-helix13-153
α-helix22-3514
α-helix42-8847
α-helix96-13742
α-helix143-1519
α-helix160-17718
β-strand186-19163
β-strand197-20153
α-helix205-2073
β-strand212-21763
α-helix225-25026
α-helix253-2542
β-strand258-26253
β-strand270-27563
α-helix276-2783
α-helix284-30118
β-strand306-30943
α-helix321-33818
β-strand346-35053
α-helix354-36512

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Vacuolar transporter chaperone 4,Core histone macro-H2A.1A, Bprotein374Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Homo sapiensO75367 (AlphaFold model), P47075 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5LNC_1 Vacuolar transporter chaperone 4,Core histone macro-H2A.1 (chains A, B)
MKFGEHLSKSLIRQYSYYYISYDDLKTELEDNLSKNNGQWTQELETDFLESLEIELDKVY
TFCKVKHSEVFRRVKEVQEQVQHTVRLLDSNNPPTQLDFEILEEELSDIIADVHDLAKFS
RLNYTGFQKIIKKHDKKTGFILKPVFQVRLDSKPFFKENYDELVVKISQLYDIARTSGAG
SDGFTVLSTKSLFLGQKLQVVQADIASIDSDAVVHPTNTDFYIGGEVGNTLEKKGGKEFV
EAVLELRKKNGPLEVAGAAVSAGHGLPAKFVIHCNSPVWGADKCEELLEKTVKNCLALAD
DKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFVSTMSSSIKTVYFVLFDSESIGIY
VQEMAKLEHHHHHH

Primary citation

The macro domain as fusion tag for carrier-driven crystallization. Wild, R., Hothorn, M. Protein Sci (2017) 26:365-374. DOI 10.1002/pro.3073 · PubMed

Other PDB entries of the same protein (UniProt O75367 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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