1CM8: Phosphorylated map kinase P38-gamma

Phosphorylated map kinase P38-gamma. Determined by X-ray diffraction at 2.4 Å resolution. Released 17 May 2000.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,442
Mol. weight: 85.42 kDa
Ligands: ANP, MG
Released: 17 May 2000

Explore 1CM8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1CM8 contains 36 α-helices and 32 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: 18 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	11	1	1
β-strand	14-15	2	2
β-strand	20-21	2	2
β-strand	24	1	1
β-strand	27-32	6	3
β-strand	41-46	6	3
β-strand	52-57	6	3
α-helix	65-80	16
β-strand	83	1	4
β-strand	86	1	4
β-strand	91-93	3	3
β-strand	106-110	5	3
β-strand	114-115	2	4
α-helix	116-122	7
α-helix	127-146	20
β-strand	149-150	2	5
α-helix	156-158	3
β-strand	159-161	3	4
β-strand	167-169	3	4
β-strand	176-177	2	5
α-helix	189-191	3
α-helix	195-198	4
α-helix	207-221	15
α-helix	231-242	12
α-helix	244-246	3
α-helix	247-251	5
α-helix	256-264	9
α-helix	270-272	3
α-helix	273-275	3
α-helix	282-291	10
α-helix	300-301	2
α-helix	302-307	6
α-helix	309-311	3
α-helix	337-349	13

Chain B: 18 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	1011	1	6
β-strand	1014-1015	2	7
β-strand	1020-1021	2	7
β-strand	1024	1	6
β-strand	1027-1032	6	8
β-strand	1041-1046	6	8
β-strand	1052-1057	6	8
α-helix	1065-1080	16
β-strand	1083	1	9
β-strand	1086	1	9
β-strand	1091-1093	3	8
β-strand	1106-1110	5	8
β-strand	1114-1115	2	9
α-helix	1116-1122	7
α-helix	1127-1146	20
β-strand	1149-1150	2	10
α-helix	1156-1158	3
β-strand	1159-1161	3	9
β-strand	1167-1169	3	9
β-strand	1176-1177	2	10
α-helix	1189-1191	3
α-helix	1195-1198	4
α-helix	1207-1221	15
α-helix	1231-1242	12
α-helix	1244-1246	3
α-helix	1247-1251	5
α-helix	1256-1264	9
α-helix	1268-1272	5
α-helix	1273-1275	3
α-helix	1282-1291	10
α-helix	1300-1301	2
α-helix	1302-1307	6
α-helix	1309-1311	3
α-helix	1337-1349	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Phosphorylated map kinase P38-gamma	A, B	protein	367	Homo sapiens	P53778 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1CM8_1 PHOSPHORYLATED MAP KINASE P38-GAMMA (chains A, B)
MSSPPPARSGFYRQEVTKTAWEVRAVYRDLQPVGSGAYGAVCSAVDGRTGAKVAIKKLYR
PFQSELFAKRAYRELRLLKHMRHENVIGLLDVFTPDETLDDFTDFYLVMPFMGTDLGKLM
KHEKLGEDRIQFLVYQMLKGLRYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQADS
EMTGYVVTRWYRAPEVILNWMRYTQTVDIWSVGCIMAEMITGKTLFKGSDHLDQLKEIMK
VTGTPPAEFVQRLQSDEAKNYMKGLPELEKKDFASILTNASPLAVNLLEKMLVLDAEQRV
TAGEALAHPYFESLHDTEDEPQVQKYDDSFDDVDRTLDEWKRVTYKEVLSFKPPRQLGAR
VSKETPL

Ligands and cofactors

ID	Name	Formula	Copies
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	2
MG	Magnesium ion	Mg	4

Primary citation

The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation. Bellon, S., Fitzgibbon, M.J., Fox, T. et al. Structure (1999) 7:1057-1065. DOI 10.1016/S0969-2126(99)80173-7 · PubMed

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

4QUM 2.52 Å, Crystal structure of PTPN3 (PTPH1) in complex with a dually phosphorylated MAPK12 peptide
6UNA 2.55 Å, Crystal structure of inactive p38gamma
7CGA 3.15 Å, Crystal structure of human unphosphorylated p38gamma

Browse structure collections

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