5IIT: PDB entry 5IIT

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 2.13 Å resolution. Released 27 Apr 2016.

Method
X-ray diffraction
Resolution
2.13 Å
Organisms
Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Homo sapiens
Chains
4
Atoms
11,622
Mol. weight
170.46 kDa
Ligands
MG
Released
27 Apr 2016

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

Secondary structure: helices and β-sheets

5IIT contains 52 α-helices and 36 β-strands across 4 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-helix15-184
α-helix21-3515
α-helix42-8948
β-strand9511
α-helix96-13843
α-helix143-15210
β-strand15712
α-helix160-17516
α-helix1841
β-strand185-19173
β-strand197-20263
α-helix205-2073
β-strand212-21653
α-helix226-25025
α-helix253-2542
β-strand258-26253
β-strand270-27453
α-helix276-2783
α-helix284-30118
β-strand306-30943
α-helix321-33818
β-strand346-35163
α-helix354-36613
Chain B: 14 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix15-184
α-helix21-3515
α-helix42-8948
β-strand9514
α-helix96-13843
α-helix143-15210
β-strand15715
α-helix160-17516
α-helix1841
β-strand185-19176
β-strand197-20266
α-helix205-2073
β-strand212-21656
α-helix225-25026
α-helix253-2542
β-strand258-26256
β-strand270-27456
α-helix276-2783
α-helix284-30118
β-strand306-30946
α-helix321-33818
β-strand346-35166
α-helix354-36613
Chain C: 12 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix15-184
α-helix21-3515
α-helix42-8948
β-strand9515
α-helix96-13843
α-helix143-15210
β-strand15714
α-helix160-17516
α-helix1841
β-strand185-19177
β-strand197-20267
β-strand212-21657
α-helix226-25025
β-strand258-26257
β-strand270-27457
α-helix276-2783
α-helix284-30118
β-strand306-30947
α-helix321-33818
β-strand346-35057
α-helix354-36613
Chain D: 12 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix15-184
α-helix21-3515
α-helix42-8948
β-strand9512
α-helix96-13843
α-helix143-15210
β-strand15711
α-helix160-17516
α-helix1841
β-strand185-19178
β-strand197-20268
β-strand212-21768
α-helix225-25026
β-strand258-26258
β-strand270-27568
α-helix276-2783
α-helix284-30118
β-strand306-30948
α-helix321-33818
β-strand346-35058
α-helix354-36613

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Vacuolar transporter chaperone 4,Core histone macro-H2A.1A, B, C, Dprotein374Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Homo sapiensO75367 (AlphaFold model), P47075 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>5IIT_1 Vacuolar transporter chaperone 4,Core histone macro-H2A.1 (chains A, B, C, D)
MKFGEHLSKSLIRQYSYYYISYDDLKTELEDNLSKNNGQWTQELETDFLESLEIELDKVY
TFCKVKHSEVFRRVKEVQEQVQHTVRLLDSNNPPTQLDFEILEEELSDIIADVHDLAKFS
RLNYTGFQKIIKKHDKKTGFILKPVFQVRLDSKPFFKENYDELVVKISQLYDIARTSGAG
SDGFTVLSTKSLFLGQKLQVVQADIASIDSDAVVHPTNTDFYIGGEVGNTLEKKGGKEFV
EAVLELRKKNGPLEVAGAAVSAGHGLPAKFVIHCNSPVWGADKCEELLEKTVKNCLALAD
DKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFVSTMSSSIKTVYFVLFDSESIGIY
VQEMAKLEHHHHHH

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg2

Water and common crystallization additives (EDO, SO4, MES) are not listed.

Primary citation

Control of eukaryotic phosphate homeostasis by inositol polyphosphate sensor domains. Wild, R., Gerasimaite, R., Jung, J.Y. et al. Science (2016) 352:986-990. DOI 10.1126/science.aad9858 · 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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