2YPI: Triosephosphate isomerase

Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-Å resolution. Implications for catalysis. Determined by X-ray diffraction at 2.5 Å resolution. Released 15 Jan 1991.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Saccharomyces cerevisiae
Chains: 2
Atoms: 3,809
Mol. weight: 53.7 kDa
Ligands: PGA
Released: 15 Jan 1991

Explore 2YPI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2YPI contains 27 α-helices and 24 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: 13 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	6-10	5	1
β-strand	13	1	2
α-helix	17-29	13
β-strand	37-41	5	1
α-helix	44-46	3
α-helix	47-53	7
β-strand	59-61	3	1
β-strand	72	1	3
α-helix	80-85	6
β-strand	92-93	2	1
α-helix	96-99	4
α-helix	106-118	13
β-strand	123-127	5	1
α-helix	131-135	5
α-helix	140-151	12
β-strand	160-164	5	1
α-helix	175-177	3
α-helix	178-196	19
α-helix	198-203	6
β-strand	205-208	4	1
α-helix	215-220	6
β-strand	228-231	4	1
α-helix	240-244	5

Chain B: 14 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	5-10	6	4
β-strand	13	1	3
α-helix	19-29	11
β-strand	36-41	6	4
α-helix	47-53	7
β-strand	59-61	3	4
β-strand	62-63	2	5
β-strand	67	1	6
β-strand	72	1	2
β-strand	79	1	6
α-helix	80-85	6
β-strand	90-91	2	5
β-strand	92-93	2	4
α-helix	96-101	6
α-helix	106-118	13
β-strand	123-127	5	4
α-helix	131-135	5
α-helix	141-151	11
β-strand	160-164	5	4
α-helix	167-169	3
α-helix	175-177	3
α-helix	178-191	14
α-helix	198-203	6
β-strand	206-208	3	4
α-helix	216-220	5
β-strand	228-231	4	4
α-helix	233-236	4
α-helix	239-243	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Triosephosphate isomerase	A, B	protein	247	Saccharomyces cerevisiae	P00942 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2YPI_1 TRIOSEPHOSPHATE ISOMERASE (chains A, B)
ARTFFVGGNFKLNGSKQSIKEIVERLNTASIPENVEVVICPPATYLDYSVSLVKKPQVTV
GAQNAYLKASGAFTGENSVDQIKDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGV
GVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKDWTNVVVAYEPVWAIGTGLAATPEDA
QDIHASIRKFLASKLGDKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPEFV
DIINSRN

Ligands and cofactors

ID	Name	Formula	Copies
PGA	2-phosphoglycolic acid	C2 H5 O6 P	2

Primary citation

Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis. Lolis, E., Petsko, G.A. Biochemistry (1990) 29:6619-6625. DOI 10.1021/bi00480a010 · 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
1I45 1.8 Å, Yeast triosephosphate isomerase (MUTANT)
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…
3YPI 2.8 Å, Electrophilic catalysis in triosephosphase isomerase: the role of histidine-95

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