1NF0: Triosephosphate Isomerase

Name: PDB 1NF0: Triosephosphate Isomerase in Complex with DHAP
Published: 2003-01-07
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: isomerase

Triosephosphate Isomerase in Complex with DHAP. Determined by X-ray diffraction at 1.6 Å resolution. Released 7 Jan 2003.

Method: X-ray diffraction
Resolution: 1.6 Å
Organism: Saccharomyces cerevisiae
Chains: 2
Atoms: 4,304
Mol. weight: 53.64 kDa
Ligands: 13P
Released: 7 Jan 2003

Explore 1NF0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1NF0 contains 31 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
α-helix	3-5	3
β-strand	6-10	5	1
β-strand	13	1	2
α-helix	17-28	12
β-strand	37-41	5	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	139-151	13
β-strand	160-164	5	1
α-helix	167-169	3
α-helix	175-177	3
α-helix	178-196	19
α-helix	198-203	6
β-strand	206-208	3	1
α-helix	217-220	4
β-strand	228-231	4	1
α-helix	233-236	4
α-helix	240-244	5

Chain B: 15 helices, 10 β-strands

Element	Residues	Length	Sheet
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	96-101	6
α-helix	106-118	13
β-strand	122-127	6	4
α-helix	131-135	5
α-helix	139-151	13
β-strand	160-164	5	4
α-helix	167-169	3
α-helix	175-177	3
α-helix	178-196	19
α-helix	198-203	6
β-strand	206-209	4	4
α-helix	217-220	4
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	247	Saccharomyces cerevisiae	P00942 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1NF0_1 triosephosphate isomerase (chains A, B)
ARTFFVGGNFKLNGSKQSIKEIVERLNTASIPENVEVVICPPATYLDYSVSLVKKPQVTV
GAQNAYLKASGAFTGENSVDQIKDVGAKYVILGHSERRSYFHEDDKFIADKTKFALGQGV
GVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKDFTNVVVAYEPVWAIGTGLAATPEDA
QDIHASIRKFLASKLGDKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPEFV
DIINSRN

Ligands and cofactors

ID	Name	Formula	Copies
13P	1,3-dihydroxyacetonephosphate	C3 H7 O6 P	2

Primary citation

Optimal alignment for enzymatic proton transfer: Structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution. Jogl, G., Rozovsky, S., McDermott, A.E. et al. Proc Natl Acad Sci U S A (2003) 100:50-55. DOI 10.1073/pnas.0233793100 · 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
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…
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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