1I45: Yeast triosephosphate isomerase

Name: PDB 1I45: Yeast triosephosphate isomerase (MUTANT)
Published: 2001-06-30
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: isomerase

Yeast triosephosphate isomerase (MUTANT). Determined by X-ray diffraction at 1.8 Å resolution. Released 30 Jun 2001.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Saccharomyces cerevisiae
Chains: 2
Atoms: 4,387
Mol. weight: 53.57 kDa
Released: 30 Jun 2001

Explore 1I45 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1I45 contains 30 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
α-helix	3-4	2
β-strand	5-10	6	1
β-strand	13	1	2
α-helix	17-29	13
β-strand	36-41	6	1
α-helix	44-46	3
α-helix	47-53	7
β-strand	59-63	5	1
β-strand	72	1	3
α-helix	80-85	6
β-strand	90-93	4	1
α-helix	96-101	6
α-helix	106-118	13
β-strand	122-127	6	1
α-helix	131-135	5
α-helix	139-153	15
β-strand	160-164	5	1
α-helix	167-169	3
α-helix	178-196	19
α-helix	198-203	6
β-strand	205-208	4	1
α-helix	217-220	4
β-strand	228-231	4	1
α-helix	233-236	4
α-helix	239-244	6

Chain B: 15 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	3-4	2
β-strand	5-10	6	4
β-strand	13	1	3
α-helix	17-29	13
β-strand	36-41	6	4
α-helix	44-46	3
α-helix	47-53	7
β-strand	59-63	5	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	139-153	15
β-strand	160-164	5	4
α-helix	167-169	3
α-helix	178-196	19
α-helix	198-203	6
β-strand	205-208	4	4
α-helix	217-220	4
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	248	Saccharomyces cerevisiae	P00942 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1I45_1 TRIOSEPHOSPHATE ISOMERASE (chains A, B)
MARTFFVGGNFKLNGSKQSIKEIVERLNTASIPENVEVVICPPATYLDYSVSLVKKPQVT
VGAQNAYLKASGAFTGENSVDQIKDVGAKYVILGHSERRSYFHEDDKFIADKTKFALGQG
VGVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKDFTNVVVAYEPVWAIGTGLAATPED
AQDIHASIRKFLASKLGDKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPEF
VDIINSRN

Primary citation

Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics. Rozovsky, S., Jogl, G., Tong, L. et al. J Mol Biol (2001) 310:271-280. DOI 10.1006/jmbi.2001.4673 · PubMed

Other PDB entries of the same protein (UniProt P00942 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1NEY 1.2 Å, Triosephosphate Isomerase in Complex with DHAP
1NF0 1.6 Å, Triosephosphate Isomerase in Complex with DHAP
4FF7 1.86 Å, Structure of C126S mutant of Saccharomyces cerevisiae triosephosphate isomerase
1YPI 1.9 Å, Structure of yeast triosephosphate isomerase at 1.9-Å resolution
7TIM 1.9 Å, Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an…
2YPI 2.5 Å, Crystallographic analysis of the complex between triosephosphate isomerase and…
3YPI 2.8 Å, Electrophilic catalysis in triosephosphase isomerase: the role of histidine-95

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