1TPB: Triosephosphate isomerase

Offset of a catalytic lesion by a bound water soluble. Determined by X-ray diffraction at 1.9 Å resolution. Released 14 Feb 1995.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Gallus gallus
Chains: 2
Atoms: 3,983
Mol. weight: 53.39 kDa
Ligands: PGH
Released: 14 Feb 1995

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

Secondary structure: helices and β-sheets

1TPB 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 1: 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	80-86	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	131-135	5
α-helix	139-151	13
α-helix	157-159	3
β-strand	160-164	5	1
α-helix	167-169	3
α-helix	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 2: 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	1, 2	protein	247	Gallus gallus	P00940 (AlphaFold model)

Sequence of entity 1 (1, 2), FASTA

>1TPB_1 TRIOSEPHOSPHATE ISOMERASE (chains 1, 2)
APRKFFVGGNWKMNGDKKSLGELIHTLNGAKLSADTEVVCGAPSIYLDFARQKLDAKIGV
AAQNCYKVPKGAFTGEISPAMIKDIGAAWVILGHSERRHVFGESDELIGQKVAHALAEGL
GVIACIGEKLDEREAGITEKVVFEQTKAIADNVKDWSKVVLAYDPVWAIGTGKTATPQQA
QEVHEKLRGWLKTHVSDAVAQSTRIIYGGSVTGGNCKELASQHDVDGFLVGGASLKPEFV
DIINAKH

Ligands and cofactors

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

Primary citation

The structural basis for pseudoreversion of the E165D lesion by the secondary S96P mutation in triosephosphate isomerase depends on the positions of active site water molecules. Komives, E.A., Lougheed, J.C., Liu, K. et al. Biochemistry (1995) 34:13612-13621. DOI 10.1021/bi00041a041 · 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…
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
1TPW 1.9 Å, Triosephosphate isomerase drinks water to keep healthy
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

Browse structure collections

About this viewer

MolViewer shows 1TPB directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.