2JK2: Triosephosphate isomerase

Name: PDB 2JK2: Structural basis of human triosephosphate isomerase deficiency. Crystal structure of the wild type enzyme.
Published: 2008-07-01
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: isomerase

Structural basis of human triosephosphate isomerase deficiency. Crystal structure of the wild type enzyme. Determined by X-ray diffraction at 1.7 Å resolution. Released 1 Jul 2008.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 3,984
Mol. weight: 53.43 kDa
Released: 1 Jul 2008

Explore 2JK2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2JK2 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: 15 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	80-85	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	139-152	14
α-helix	157-159	3
β-strand	160-164	5	1
α-helix	167-169	3
α-helix	178-193	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	239-244	6

Chain B: 15 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
β-strand	37-42	6	4
α-helix	45-47	3
α-helix	48-54	7
β-strand	60-63	4	4
β-strand	72	1	2
α-helix	80-85	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	131-135	5
α-helix	139-152	14
α-helix	157-159	3
β-strand	160-164	5	4
α-helix	178-195	18
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	250	HOMO SAPIENS	P60174 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2JK2_1 TRIOSEPHOSPHATE ISOMERASE (chains A, B)
GSAPSRKFFVGGNWKMNGRKQSLGELIGTLNAAKVPADTEVVCAPPTAYIDFARQKLDPK
IAVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALA
EGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATP
QQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKP
EFVDIINAKQ

Primary citation

Structural Basis of Human Triosephosphate Isomerase Deficiency: Mutation E104D is Related to Alterations of a Conserved Water Network at the Dimer Interface. Rodriguez-Almazan, C., Arreola, R., Rodriguez-Larrea, D. et al. J Biol Chem (2008) 283:23254. DOI 10.1074/JBC.M802145200 · 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
7RDE 1.31 Å, Human Triose Phosphate Isomerase Q181P
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
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

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