4POD: Triosephosphate isomerase

Name: PDB 4POD: Structure of Triosephosphate Isomerase I170V mutant human enzyme.
Published: 2015-01-14
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: isomerase

Structure of Triosephosphate Isomerase I170V mutant human enzyme. Determined by X-ray diffraction at 1.99 Å resolution. Released 14 Jan 2015.

Method: X-ray diffraction
Resolution: 1.99 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,970
Mol. weight: 54.7 kDa
Ligands: PO4
Released: 14 Jan 2015

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

Secondary structure: helices and β-sheets

4POD contains 33 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: 16 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	139-151	13
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
α-helix	245-247	3

Chain B: 17 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	4-5	2
β-strand	6-11	6	4
β-strand	14	1	3
α-helix	18-31	14
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	175-177	3
α-helix	178-195	18
α-helix	198-203	6
β-strand	206-209	4	4
α-helix	217-221	5
β-strand	228-231	4	4
α-helix	233-236	4
α-helix	240-244	5

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

>4POD_1 Triosephosphate isomerase (chains A, B)
GDITHMAPSRKFFVGGNWKMNGRKQSLGELIGTLNAAKVPADTEVVCAPPTAYIDFARQK
LDPKIAVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVA
HALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAVGTGK
TATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGA
SLKPEFVDIINAKQ

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	1

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:

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
4ZVJ 1.7 Å, Structure of human triose phosphate isomerase K13M
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

Browse structure collections

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