7RDE: Human Triose Phosphate Isomerase Q181P

Name: PDB 7RDE: Human Triose Phosphate Isomerase Q181P
Published: 2022-05-04
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: isomerase

Human Triose Phosphate Isomerase Q181P. Determined by X-ray diffraction at 1.31 Å resolution. Released 4 May 2022.

Method: X-ray diffraction
Resolution: 1.31 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,170
Mol. weight: 53.54 kDa
Ligands: CA
Released: 4 May 2022

Explore 7RDE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7RDE 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: 14 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	6-11	6	1
β-strand	14	1	2
α-helix	18-31	14
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	80-85	6
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	180-195	16
α-helix	198-203	6
β-strand	206-208	3	1
α-helix	217-221	5
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
α-helix	4-5	2
β-strand	6-11	6	4
β-strand	14	1	3
α-helix	18-30	13
α-helix	33-34	2
β-strand	37-42	6	4
α-helix	45-47	3
α-helix	48-54	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	131-136	6
α-helix	139-151	13
α-helix	157-159	3
β-strand	160-164	5	4
α-helix	181-195	15
α-helix	198-203	6
β-strand	206-208	3	4
α-helix	217-221	5
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	249	Homo sapiens	P60174 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7RDE_1 Triosephosphate isomerase (chains A, B)
MAPSRKFFVGGNWKMNGRKQSLGELIGTLNAAKVPADTEVVCAPPTAYIDFARQKLDPKI
AVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAE
GLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQ
PAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE
FVDIINAKQ

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	1

Water and common crystallization additives (BR) are not listed.

Primary citation

Itavastatin and resveratrol increase triosephosphate isomerase protein in a newly identified variant of TPI deficiency. VanDemark, A.P., Hrizo, S.L., Eicher, S.L. et al. Dis Model Mech (2022) 15. DOI 10.1242/dmm.049261 · PubMed

Other PDB entries of the same protein (UniProt P60174 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9F69 1.17 Å, Crystal structure of human triose phosphate isomerase with methyl malonic acid ligand
9FFC 1.25 Å, Crystal structure of human triose phosphate isomerase with glycerol-3-phosphate ligand
4UNL 1.5 Å, Crystal structure of a single mutant (N71D) of triosephosphate isomerase from human
4POC 1.6 Å, Structure of Triosephosphate Isomerase Wild Type human enzyme.
6UPF 1.65 Å, Triosephosphate isomerase deficiency: Effect of F240L mutation on enzyme structure
4ZVJ 1.7 Å, Structure of human triose phosphate isomerase K13M
2JK2 1.7 Å, Structural basis of human triosephosphate isomerase deficiency. Crystal structure of the…
6UP1 1.83 Å, Triosephosphate isomerase deficiency: Effect of F240L mutation on enzyme structure
2VOM 1.85 Å, Structural basis of human triosephosphate isomerase deficiency. Mutation E104D and…
4BR1 1.9 Å, Protease-induced heterodimer of human triosephosphate isomerase.
6UP5 1.92 Å, Triosephosphate isomerase deficiency: Effect of F240L mutation on enzyme structure
1KLU 1.93 Å, Crystal structure of HLA-DR1/TPI(23-37) complexed with staphylococcal enterotoxin C3…

Browse structure collections

About this viewer

MolViewer shows 7RDE 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.