8G17: Wild-type GAPDH

CryoEM structure of wild-type GAPDH. Determined by electron microscopy at 1.98 Å resolution. Released 27 Dec 2023.

Method: Electron microscopy
Resolution: 1.98 Å
Organism: Homo sapiens
Chains: 4
Atoms: 10,016
Mol. weight: 143.87 kDa
Released: 27 Dec 2023

Explore 8G17 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8G17 contains 60 α-helices and 80 β-strands across 4 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.

Chains A, B, C and D: 15 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	3-4	2
β-strand	5-9	5	1
α-helix	13-25	13
β-strand	29-34	6	1
α-helix	40-48	9
β-strand	60-63	4	2
β-strand	66-69	4	2
β-strand	72-74	3	2
β-strand	75-77	3	1
α-helix	82-84	3
α-helix	87-90	4
β-strand	94-97	4	1
α-helix	105-108	4
α-helix	110-113	4
β-strand	118-121	4	1
β-strand	130	1	1
α-helix	137-139	3
β-strand	146-148	3	1
α-helix	152-168	17
β-strand	170-179	10	3
β-strand	186	1	4
α-helix	197-199	3
β-strand	201	1	4
β-strand	208-210	3	3
α-helix	213-220	8
α-helix	222-224	3
β-strand	228-234	7	3
β-strand	241-249	9	3
α-helix	255-267	13
β-strand	274-277	4	3
α-helix	283-286	4
β-strand	293-296	4	3
β-strand	301-304	4	3
β-strand	307-314	8	3
α-helix	318-333	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glyceraldehyde-3-phosphate dehydrogenase	A, B, C, D	protein	334	Homo sapiens	P04406 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>8G17_1 Glyceraldehyde-3-phosphate dehydrogenase (chains A, B, C, D)
GKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVK
AENGKLVINGNPITIFQERDPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVII
SAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAI
TATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVS
VVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGI
ALNDHFVKLISWYDNEFGYSNRVVDLMAHMASKE

Primary citation

Efficient tagging of endogenous proteins in human cell lines for structural studies by single-particle cryo-EM. Choi, W., Wu, H., Yserentant, K. et al. Proc Natl Acad Sci U S A (2023) 120:e2302471120-e2302471120. DOI 10.1073/pnas.2302471120 · PubMed

Other PDB entries of the same protein (UniProt P04406 (AlphaFold model), which also has an AlphaFold model), best resolution first:

27FM 1.46 Å, Crystal structure of human glyceraldehyde-3-phosphate dehydrogenase bound to gold(I)
6YND 1.52 Å, GAPDH purified from the supernatant of HEK293F cells: crystal form 1 of 4.
1U8F 1.75 Å, Crystal Structure Of Human Placental Glyceraldehyde-3-Phosphate Dehydrogenase At 1.75…
9L3E 1.77 Å, Structure of GAPDH complexed with Leu-F
8P5F 1.82 Å, Human wild-type GAPDH,orthorhombic form
6M61 1.82 Å, Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) with inhibitor heptelidic acid
6YNE 1.85 Å, GAPDH purified from the supernatant of HEK293F cells: crystal form 2 of 4.
9UNY 1.87 Å, Natural product inhibitor of glyceraldehyde-3-phosphate dehydrogenase(GAPDH)
4WNC 1.99 Å, Crystal structure of human wild-type GAPDH at 1.99 angstroms resolution
8G15 2.07 Å, CryoEM structure of nuclear GAPDH under 24h Oxidative Stress
8G16 2.07 Å, CryoEM structure of cytoplasmic GAPDH under 24h Oxidative Stress
8G12 2.17 Å, CryoEM structure of nuclear GAPDH under 8h Oxidative Stress

Browse structure collections

About this viewer

MolViewer shows 8G17 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.