4ZVJ: Human triose phosphate isomerase K13M

Name: PDB 4ZVJ: Structure of human triose phosphate isomerase K13M
Published: 2016-03-09
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: isomerase

Structure of human triose phosphate isomerase K13M. Determined by X-ray diffraction at 1.7 Å resolution. Released 9 Mar 2016.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,114
Mol. weight: 54.52 kDa
Released: 9 Mar 2016

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

Secondary structure: helices and β-sheets

4ZVJ contains 32 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: 15 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	6-11	6	1
β-strand	14	1	2
α-helix	18-30	13
β-strand	37-42	6	1
α-helix	45-47	3
α-helix	48-54	7
β-strand	60-63	4	1
β-strand	72	1	3
α-helix	80-85	6
β-strand	90-93	4	1
α-helix	96-100	5
α-helix	106-118	13
β-strand	122-127	6	1
α-helix	131-135	5
α-helix	139-152	14
α-helix	157-159	3
β-strand	160-164	5	1
α-helix	167-169	3
α-helix	178-195	18
α-helix	198-203	6
β-strand	206-208	3	1
α-helix	217-221	5
β-strand	228-231	4	1
α-helix	233-236	4
α-helix	239-244	6

Chain B: 17 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	3-5	3
β-strand	6-11	6	4
β-strand	14	1	3
α-helix	18-30	13
α-helix	33-34	2
β-strand	37-42	6	4
α-helix	45-47	3
α-helix	48-54	7
β-strand	60-63	4	4
β-strand	72	1	2
α-helix	80-85	6
β-strand	90-93	4	4
α-helix	96-100	5
α-helix	106-118	13
β-strand	122-127	6	4
α-helix	131-135	5
α-helix	139-151	13
α-helix	157-159	3
β-strand	160-164	5	4
α-helix	167-169	3
α-helix	178-195	18
α-helix	198-203	6
β-strand	206-208	3	4
α-helix	217-221	5
β-strand	228-231	4	4
α-helix	233-236	4
α-helix	239-244	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Triosephosphate isomerase	A, B	protein	254	Homo sapiens	P60174 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4ZVJ_1 Triosephosphate isomerase (chains A, B)
GDITHMAPSRKFFVGGNWMMNGRKQSLGELIGTLNAAKVPADTEVVCAPPTAYIDFARQK
LDPKIAVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVA
HALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGK
TATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGA
SLKPEFVDIINAKQ

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:

9F69 1.17 Å, Crystal structure of human triose phosphate isomerase with methyl malonic acid ligand
9FFC 1.25 Å, Crystal structure of human triose phosphate isomerase with glycerol-3-phosphate ligand
7RDE 1.31 Å, Human Triose Phosphate Isomerase Q181P
4UNL 1.5 Å, Crystal structure of a single mutant (N71D) of triosephosphate isomerase from human
4POC 1.6 Å, Structure of Triosephosphate Isomerase Wild Type human enzyme.
6UPF 1.65 Å, Triosephosphate isomerase deficiency: Effect of F240L mutation on enzyme structure
2JK2 1.7 Å, Structural basis of human triosephosphate isomerase deficiency. Crystal structure of the…
6UP1 1.83 Å, Triosephosphate isomerase deficiency: Effect of F240L mutation on enzyme structure
2VOM 1.85 Å, Structural basis of human triosephosphate isomerase deficiency. Mutation E104D and…
4BR1 1.9 Å, Protease-induced heterodimer of human triosephosphate isomerase.
6UP5 1.92 Å, Triosephosphate isomerase deficiency: Effect of F240L mutation on enzyme structure
1KLU 1.93 Å, Crystal structure of HLA-DR1/TPI(23-37) complexed with staphylococcal enterotoxin C3…

Browse structure collections

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