6IQ6: GAPDH
Crystal structure of GAPDH. Determined by X-ray diffraction at 2.29 Å resolution. Released 28 Aug 2019.
- Method
- X-ray diffraction
- Resolution
- 2.29 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 20,298
- Mol. weight
- 289.44 kDa
- Ligands
- AW9
- Released
- 28 Aug 2019
Explore 6IQ6 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6IQ6 contains 114 α-helices and 147 β-strands across 8 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: 13 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| 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 | |
| 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 | 170-180 | 11 | 3 |
| α-helix | 196-199 | 4 | |
| β-strand | 207-210 | 4 | 3 |
| α-helix | 213-220 | 8 | |
| α-helix | 222-224 | 3 | |
| β-strand | 228-235 | 8 | 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 | 318-332 | 15 | |
Chain B: 15 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-9 | 5 | 4 |
| α-helix | 13-25 | 13 | |
| β-strand | 29-34 | 6 | 4 |
| α-helix | 40-48 | 9 | |
| β-strand | 60-63 | 4 | 4 |
| β-strand | 66-69 | 4 | 4 |
| β-strand | 72-77 | 6 | 4 |
| α-helix | 82-84 | 3 | |
| α-helix | 87-90 | 4 | |
| β-strand | 94-97 | 4 | 4 |
| α-helix | 105-108 | 4 | |
| α-helix | 109-112 | 4 | |
| β-strand | 118-121 | 4 | 4 |
| β-strand | 130 | 1 | 4 |
| α-helix | 137-139 | 3 | |
| β-strand | 146-148 | 3 | 4 |
| α-helix | 152-168 | 17 | |
| β-strand | 170-179 | 10 | 5 |
| β-strand | 186 | 1 | 6 |
| α-helix | 196-199 | 4 | |
| β-strand | 201 | 1 | 6 |
| β-strand | 207-210 | 4 | 5 |
| α-helix | 213-220 | 8 | |
| α-helix | 222-224 | 3 | |
| β-strand | 228-234 | 7 | 5 |
| β-strand | 241-249 | 9 | 5 |
| α-helix | 255-267 | 13 | |
| β-strand | 274-277 | 4 | 5 |
| α-helix | 283-286 | 4 | |
| β-strand | 293-296 | 4 | 5 |
| α-helix | 297-299 | 3 | |
| β-strand | 301-304 | 4 | 5 |
| β-strand | 307-314 | 8 | 5 |
| α-helix | 318-333 | 16 | |
Chain C: 14 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-9 | 5 | 7 |
| α-helix | 13-25 | 13 | |
| β-strand | 29-34 | 6 | 7 |
| α-helix | 40-48 | 9 | |
| β-strand | 60-63 | 4 | 7 |
| β-strand | 66-69 | 4 | 7 |
| β-strand | 72-77 | 6 | 7 |
| α-helix | 82-84 | 3 | |
| α-helix | 87-90 | 4 | |
| β-strand | 94-97 | 4 | 7 |
| α-helix | 105-108 | 4 | |
| α-helix | 110-113 | 4 | |
| β-strand | 118-121 | 4 | 7 |
| β-strand | 130 | 1 | 7 |
| α-helix | 137-139 | 3 | |
| β-strand | 146-148 | 3 | 7 |
| α-helix | 152-167 | 16 | |
| β-strand | 170-179 | 10 | 8 |
| β-strand | 186 | 1 | 9 |
| α-helix | 196-199 | 4 | |
| β-strand | 201 | 1 | 9 |
| β-strand | 207-210 | 4 | 8 |
| α-helix | 213-220 | 8 | |
| α-helix | 222-224 | 3 | |
| β-strand | 228-234 | 7 | 8 |
| β-strand | 241-249 | 9 | 8 |
| α-helix | 255-267 | 13 | |
| β-strand | 274-277 | 4 | 8 |
| α-helix | 283-286 | 4 | |
| β-strand | 293-296 | 4 | 8 |
| β-strand | 301-304 | 4 | 8 |
| β-strand | 307-314 | 8 | 8 |
| α-helix | 318-332 | 15 | |
Chain D: 14 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-9 | 5 | 10 |
| α-helix | 13-25 | 13 | |
| β-strand | 29-34 | 6 | 10 |
| α-helix | 40-48 | 9 | |
| β-strand | 60-63 | 4 | 10 |
| β-strand | 66-69 | 4 | 10 |
| β-strand | 72-77 | 6 | 10 |
| α-helix | 82-84 | 3 | |
| α-helix | 87-90 | 4 | |
| β-strand | 94-97 | 4 | 10 |
| α-helix | 105-108 | 4 | |
| α-helix | 110-113 | 4 | |
| β-strand | 118-121 | 4 | 10 |
| β-strand | 130 | 1 | 10 |
| α-helix | 137-139 | 3 | |
| β-strand | 146-148 | 3 | 10 |
| α-helix | 152-168 | 17 | |
| β-strand | 170-179 | 10 | 11 |
| α-helix | 196-199 | 4 | |
| β-strand | 207-210 | 4 | 11 |
| α-helix | 213-220 | 8 | |
| α-helix | 222-224 | 3 | |
| β-strand | 228-234 | 7 | 11 |
| β-strand | 241-249 | 9 | 11 |
| α-helix | 255-267 | 13 | |
| β-strand | 274-277 | 4 | 11 |
| α-helix | 283-286 | 4 | |
| β-strand | 293-296 | 4 | 11 |
| β-strand | 301-304 | 4 | 11 |
| β-strand | 307-314 | 8 | 11 |
| α-helix | 318-332 | 15 | |
Chain E: 14 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-9 | 5 | 12 |
| α-helix | 13-25 | 13 | |
| β-strand | 29-34 | 6 | 12 |
| α-helix | 40-48 | 9 | |
| β-strand | 60-63 | 4 | 13 |
| β-strand | 66-69 | 4 | 13 |
| β-strand | 72-74 | 3 | 13 |
| β-strand | 75-77 | 3 | 12 |
| α-helix | 82-84 | 3 | |
| α-helix | 87-90 | 4 | |
| β-strand | 94-97 | 4 | 12 |
| α-helix | 105-108 | 4 | |
| α-helix | 110-113 | 4 | |
| β-strand | 118-121 | 4 | 12 |
| β-strand | 130 | 1 | 12 |
| α-helix | 137-139 | 3 | |
| β-strand | 146-148 | 3 | 12 |
| α-helix | 152-167 | 16 | |
| β-strand | 170-179 | 10 | 14 |
| β-strand | 186 | 1 | 15 |
| α-helix | 196-199 | 4 | |
| β-strand | 201 | 1 | 15 |
| β-strand | 207-210 | 4 | 14 |
| α-helix | 213-220 | 8 | |
| α-helix | 222-224 | 3 | |
| β-strand | 228-234 | 7 | 14 |
| β-strand | 241-249 | 9 | 14 |
| α-helix | 255-267 | 13 | |
| β-strand | 274-277 | 4 | 14 |
| α-helix | 283-286 | 4 | |
| β-strand | 293-302 | 10 | 14 |
| β-strand | 307-314 | 8 | 14 |
| α-helix | 318-332 | 15 | |
Chain F: 15 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-9 | 5 | 16 |
| α-helix | 13-25 | 13 | |
| β-strand | 29-34 | 6 | 16 |
| α-helix | 40-48 | 9 | |
| β-strand | 60-63 | 4 | 16 |
| β-strand | 66-69 | 4 | 16 |
| β-strand | 72-77 | 6 | 16 |
| α-helix | 82-84 | 3 | |
| α-helix | 87-90 | 4 | |
| β-strand | 94-97 | 4 | 16 |
| α-helix | 105-108 | 4 | |
| α-helix | 110-113 | 4 | |
| β-strand | 118-121 | 4 | 16 |
| β-strand | 130 | 1 | 16 |
| α-helix | 137-139 | 3 | |
| β-strand | 146-148 | 3 | 16 |
| α-helix | 152-168 | 17 | |
| β-strand | 170-179 | 10 | 17 |
| α-helix | 196-199 | 4 | |
| β-strand | 207-210 | 4 | 17 |
| α-helix | 213-220 | 8 | |
| α-helix | 222-224 | 3 | |
| β-strand | 228-234 | 7 | 17 |
| β-strand | 241-249 | 9 | 17 |
| α-helix | 255-267 | 13 | |
| β-strand | 274-277 | 4 | 17 |
| α-helix | 283-286 | 4 | |
| β-strand | 293-296 | 4 | 17 |
| α-helix | 297-299 | 3 | |
| β-strand | 301-304 | 4 | 17 |
| β-strand | 307-314 | 8 | 17 |
| α-helix | 318-334 | 17 | |
Chain G: 16 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-9 | 5 | 18 |
| α-helix | 13-25 | 13 | |
| β-strand | 29-34 | 6 | 18 |
| α-helix | 40-48 | 9 | |
| β-strand | 60-63 | 4 | 19 |
| β-strand | 66-69 | 4 | 19 |
| β-strand | 72-74 | 3 | 19 |
| β-strand | 75-77 | 3 | 18 |
| α-helix | 82-84 | 3 | |
| α-helix | 87-90 | 4 | |
| β-strand | 94-97 | 4 | 18 |
| α-helix | 105-108 | 4 | |
| α-helix | 109-112 | 4 | |
| β-strand | 118-121 | 4 | 18 |
| α-helix | 129 | 1 | |
| β-strand | 130 | 1 | 18 |
| α-helix | 137-139 | 3 | |
| β-strand | 146-148 | 3 | 18 |
| α-helix | 152-168 | 17 | |
| β-strand | 170-179 | 10 | 20 |
| α-helix | 196-199 | 4 | |
| β-strand | 207-210 | 4 | 20 |
| α-helix | 217-220 | 4 | |
| α-helix | 222-224 | 3 | |
| β-strand | 228-234 | 7 | 20 |
| β-strand | 241-249 | 9 | 20 |
| α-helix | 255-267 | 13 | |
| β-strand | 274-277 | 4 | 20 |
| α-helix | 283-286 | 4 | |
| β-strand | 293-296 | 4 | 20 |
| α-helix | 297-299 | 3 | |
| β-strand | 301-304 | 4 | 20 |
| β-strand | 307-314 | 8 | 20 |
| α-helix | 318-333 | 16 | |
Chain H: 13 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-9 | 5 | 21 |
| α-helix | 13-25 | 13 | |
| β-strand | 29-34 | 6 | 21 |
| α-helix | 40-48 | 9 | |
| β-strand | 60-63 | 4 | 22 |
| β-strand | 66-69 | 4 | 22 |
| β-strand | 72-74 | 3 | 22 |
| β-strand | 75-77 | 3 | 21 |
| α-helix | 82-84 | 3 | |
| α-helix | 87-90 | 4 | |
| β-strand | 94-97 | 4 | 21 |
| α-helix | 105-113 | 9 | |
| β-strand | 118-121 | 4 | 21 |
| α-helix | 129 | 1 | |
| β-strand | 130 | 1 | 21 |
| β-strand | 146-148 | 3 | 21 |
| α-helix | 154-167 | 14 | |
| β-strand | 170-180 | 11 | 23 |
| β-strand | 186 | 1 | 24 |
| α-helix | 196-199 | 4 | |
| β-strand | 201 | 1 | 24 |
| β-strand | 207-210 | 4 | 23 |
| α-helix | 217-220 | 4 | |
| α-helix | 222-224 | 3 | |
| β-strand | 228-235 | 8 | 23 |
| β-strand | 241-249 | 9 | 23 |
| α-helix | 255-267 | 13 | |
| β-strand | 274-277 | 4 | 23 |
| α-helix | 283-286 | 4 | |
| β-strand | 293-296 | 4 | 23 |
| β-strand | 301-304 | 4 | 23 |
| β-strand | 307-314 | 8 | 23 |
| α-helix | 318-332 | 15 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Glyceraldehyde-3-phosphate dehydrogenase | A, B, C, D, E, F, G, H | protein | 335 | Homo sapiens | P04406 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA
>6IQ6_1 Glyceraldehyde-3-phosphate dehydrogenase (chains A, B, C, D, E, F, G, H)
MGKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTV
KAENGKLVINGNPITIFQERDPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVI
ISAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHA
ITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV
SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAG
IALNDHFVKLISWYDNEFGYSNRVVDLMAHMASKE
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| AW9 | (2Z)-4-methoxy-4-oxobut-2-enoic acid | C5 H6 O4 | 5 |
Primary citation
Structural Study of Monomethyl Fumarate-Bound Human GAPDH. Park, J.B., Park, H., Son, J. et al. Mol Cells (2019) 42:597-603. DOI 10.14348/molcells.2019.0114 · 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)
- 8G17 1.98 Å, CryoEM structure of wild-type 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
Browse structure collections
About this viewer
MolViewer shows 6IQ6 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.