1TPW: Triosephosphate isomerase

Triosephosphate isomerase drinks water to keep healthy. Determined by X-ray diffraction at 1.9 Å resolution. Released 20 Apr 1995.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Gallus gallus
Chains: 2
Atoms: 4,015
Mol. weight: 53.44 kDa
Ligands: PGH
Released: 20 Apr 1995

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

Secondary structure: helices and β-sheets

1TPW 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: 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	37-43	7	1
α-helix	45-47	3
α-helix	48-54	7
β-strand	60-63	4	1
β-strand	72	1	3
α-helix	80-86	7
β-strand	90-93	4	1
α-helix	96-100	5
α-helix	106-118	13
β-strand	122-127	6	1
α-helix	131-134	4
α-helix	139-151	13
α-helix	157-159	3
β-strand	160-164	5	1
α-helix	167-169	3
α-helix	175-177	3
α-helix	178-195	18
α-helix	198-203	6
β-strand	206-208	3	1
α-helix	217-222	6
β-strand	228-231	4	1
α-helix	233-236	4
α-helix	240-244	5

Chain B: 16 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	6-11	6	4
β-strand	14	1	3
α-helix	18-30	13
β-strand	37-43	7	4
α-helix	45-47	3
α-helix	48-54	7
β-strand	60-63	4	4
β-strand	72	1	2
α-helix	80-86	7
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	247	Gallus gallus	P00940 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1TPW_1 TRIOSEPHOSPHATE ISOMERASE (chains A, B)
APRKFFVGGNWKMNGDKKSLGELIHTLNGAKLSADTEVVCGAPSIYLDFARQKLDAKIGV
AAQNCYKVPKGAFTGEISPAMIKDIGAAWVILGHPERRHVFGESDELIGQKVAHALAEGL
GVIACIGEKLDEREAGITEKVVFEQTKAIADNVKDWSKVVLAYEPVWAIGTGKTATPQQA
QEVHEKLRGWLKTHVSDAVAQSTRIIYGGSVTGGNCKELASQHDVDGFLVGGASLKPEFV
DIINAKH

Ligands and cofactors

ID	Name	Formula	Copies
PGH	Phosphoglycolohydroxamic acid	C2 H6 N O6 P	2

Primary citation

The role of water in the catalytic efficiency of triosephosphate isomerase. Zhang, Z., Komives, E.A., Sugio, S. et al. Biochemistry (1999) 38:4389-4397. DOI 10.1021/bi9826759 · PubMed

Other PDB entries of the same protein (UniProt P00940 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4P61 1.34 Å, Chicken triosephosphate isomerase with LOOP6 mutations, V167P and W168E.
1SW0 1.71 Å, Triosephosphate isomerase from Gallus gallus, loop 6 hinge mutant K174L, T175W
1TPH 1.8 Å, 1.8 Å crystal structure of wild type chicken triosephosphate…
1TPB 1.9 Å, Offset of a catalytic lesion by a bound water soluble
1TPC 1.9 Å, Offset of a catalytic lesion by a bound water soluble
1TPU 1.9 Å, S96P change is a second-site suppressor for H95N sluggish mutant triosephosphate isomerase
1TPV 1.9 Å, S96P change is a second-site suppressor for H95N sluggish mutant triosephosphate isomerase
1SW3 2.03 Å, Triosephosphate isomerase from Gallus gallus, loop 6 mutant T175V
1SPQ 2.16 Å, Understanding protein lids: Structural analysis of active hinge mutants in…
1SW7 2.22 Å, Triosephosphate isomerase from Gallus gallus, loop 6 mutant K174N, T175S, A176S
1TIM 2.5 Å, Structure of triose phosphate isomerase from chicken muscle
8TIM 2.5 Å, Triose phosphate isomerase

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