7CGA: Human unphosphorylated p38gamma

Crystal structure of human unphosphorylated p38gamma. Determined by X-ray diffraction at 3.15 Å resolution. Released 30 Jun 2021.

Method
X-ray diffraction
Resolution
3.15 Å
Organism
Homo sapiens
Chains
4
Atoms
11,422
Mol. weight
159.63 kDa
Released
30 Jun 2021

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

Secondary structure: helices and β-sheets

7CGA contains 63 α-helices and 57 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.

Chain A: 18 helices, 14 β-strands

ElementResiduesLengthSheet
β-strand11-1661
β-strand19-2461
β-strand27-3592
β-strand39-4682
β-strand52-5872
α-helix65-8016
β-strand8313
β-strand8613
β-strand91-9332
α-helix99-1013
β-strand106-11052
β-strand114-11523
α-helix118-1214
α-helix129-14618
β-strand149-15024
α-helix156-1583
β-strand159-16133
β-strand167-16933
β-strand176-17724
α-helix194-1974
α-helix206-22116
α-helix231-24212
α-helix246-2494
α-helix256-2638
α-helix273-2764
α-helix282-29110
α-helix300-3012
α-helix302-3065
α-helix309-3146
α-helix324-3263
α-helix329-3324
α-helix337-34913
Chain B: 15 helices, 14 β-strands
ElementResiduesLengthSheet
β-strand11-1665
β-strand19-2465
β-strand28-3696
β-strand39-4576
β-strand52-5876
α-helix65-7915
β-strand8317
β-strand8617
β-strand91-9336
β-strand106-11056
β-strand11517
α-helix116-1227
α-helix124-1263
α-helix127-14620
β-strand149-15028
α-helix156-1583
β-strand159-16137
β-strand167-16937
β-strand176-17728
α-helix194-1974
α-helix206-22116
α-helix231-24212
α-helix256-2649
α-helix273-2764
α-helix282-29110
α-helix302-3065
α-helix309-3113
α-helix324-3263
α-helix337-35014
Chain C: 15 helices, 15 β-strands
ElementResiduesLengthSheet
β-strand11-1559
β-strand1915
β-strand20-2459
β-strand27-32610
β-strand39-46810
β-strand52-58710
α-helix65-8016
β-strand83111
β-strand86111
β-strand91-93310
α-helix99-1013
β-strand106-110510
β-strand114-115211
α-helix127-14620
β-strand149-150212
α-helix156-1583
β-strand159-161311
β-strand167-169311
β-strand176-177212
α-helix194-1974
α-helix206-22116
α-helix231-24212
α-helix247-2515
α-helix256-2638
α-helix273-2764
α-helix282-29110
α-helix302-3076
α-helix309-3113
α-helix324-3263
α-helix337-34913
Chain D: 15 helices, 14 β-strands
ElementResiduesLengthSheet
β-strand11-16613
β-strand19-24613
β-strand27-361014
β-strand39-46814
β-strand52-58714
α-helix65-7915
β-strand83115
β-strand86115
β-strand91-93314
β-strand106-110514
β-strand114-115215
α-helix116-1227
α-helix127-14620
β-strand149-150216
α-helix156-1583
β-strand159-161315
β-strand167-169315
β-strand176-177216
α-helix194-1985
α-helix207-22115
α-helix231-24212
α-helix256-2638
α-helix273-2764
α-helix282-29110
α-helix300-3012
α-helix302-3065
α-helix309-3113
α-helix324-3263
α-helix337-34913

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Mitogen-activated protein kinase 12A, B, C, Dprotein348Homo sapiensP53778 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>7CGA_1 Mitogen-activated protein kinase 12 (chains A, B, C, D)
SNASGFYRQEVTKTAWEVRAVYRDLQPVGSGAYGAVCSAVDGRTGAKVAIKKLYRPFQSE
LFAKRAYRELRLLKHMRHENVIGLLDVFTPDETLDDFTDFYLVMPFMGTDLGKLMKHEKL
GEDRIQFLVYQMLKGLRYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQADSEMTGY
VVTRWYRAPEVILNWMRYTQTVDIWSVGCIMAEMITGKTLFKGSDHLDQLKEIMKVTGTP
PAEFVQRLQSDEAKNYMKGLPELEKKDFASILTNASPLAVNLLEKMLVLDAEQRVTAGEA
LAHPYFESLHDTEDEPQVQKYDDSFDDVDRTLDEWKRVTYKEVLSFKP

Primary citation

Structural basis for allosteric regulation of protein tyrosine phosphatase PTPN3 by unphosphorylated MAP kinase p38g. Hsu, S.F., Chen, K.E., Lee, C.C. et al. To be published.

Other PDB entries of the same protein (UniProt P53778 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 7CGA 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.