4POC: Triosephosphate Isomerase Wild Type human enzyme

Structure of Triosephosphate Isomerase Wild Type human enzyme. Determined by X-ray diffraction at 1.6 Å resolution. Released 14 Jan 2015.

Method
X-ray diffraction
Resolution
1.6 Å
Organism
Homo sapiens
Chains
2
Atoms
4,056
Mol. weight
54.81 kDa
Ligands
PO4
Released
14 Jan 2015

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

Secondary structure: helices and β-sheets

4POC contains 34 α-helices and 20 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: 17 helices, 10 β-strands

ElementResiduesLengthSheet
α-helix4-52
β-strand6-1161
β-strand1412
α-helix18-3013
α-helix32-343
β-strand37-4261
α-helix45-473
α-helix48-547
β-strand60-6341
β-strand7213
α-helix80-856
β-strand90-9341
α-helix96-1005
α-helix106-11813
β-strand122-12761
α-helix131-1355
α-helix139-15113
α-helix157-1593
β-strand160-16451
α-helix167-1693
α-helix178-19518
α-helix198-2036
β-strand206-20831
α-helix217-2215
β-strand228-23141
α-helix233-2364
α-helix240-2445
Chain B: 17 helices, 10 β-strands
ElementResiduesLengthSheet
α-helix3-53
β-strand6-1164
β-strand1413
α-helix18-3013
β-strand37-4264
α-helix45-473
α-helix48-547
β-strand60-6344
β-strand7212
α-helix80-856
β-strand90-9344
α-helix96-1005
α-helix106-11813
β-strand122-12764
α-helix131-1366
α-helix139-15113
α-helix157-1593
β-strand160-16454
α-helix167-1693
α-helix175-1773
α-helix178-19518
α-helix198-2036
β-strand206-20944
α-helix217-2215
β-strand228-23144
α-helix233-2364
α-helix239-2446

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Triosephosphate isomeraseA, Bprotein254Homo sapiensP60174 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4POC_1 Triosephosphate isomerase (chains A, B)
GDITHMAPSRKFFVGGNWKMNGRKQSLGELIGTLNAAKVPADTEVVCAPPTAYIDFARQK
LDPKIAVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVA
HALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGK
TATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGA
SLKPEFVDIINAKQ

Ligands and cofactors

IDNameFormulaCopies
PO4Phosphate ionO4 P1

Water and common crystallization additives (BR, NA, K) are not listed.

Primary citation

Triosephosphate isomerase I170V alters catalytic site, enhances stability and induces pathology in a Drosophila model of TPI deficiency. Roland, B.P., Amrich, C.G., Kammerer, C.J. et al. Biochim Biophys Acta (2015) 1852:61-69. DOI 10.1016/j.bbadis.2014.10.010 · PubMed

Other PDB entries of the same protein (UniProt P60174 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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