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Fragment RZ132 in complex with MAP kinase P38-alpha

Analyse Fragment RZ132 in complex with MAP kinase P38-alpha in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SO4
Type: protein
Length: 343 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mitogen-activated protein kinase 14
EC: 2.7.11.24
UniProt: P47811
Ligands: LO8, MG, CL, SO4
Pockets: 4 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 14 (EC 2.7.11.24)	protein	343	40% helix, 15% strand	P47811

Ligands and binding sites

LO8 · (2~{S})-2-methyl-4-(oxetan-3-yl)-~{N}-(phenylmethyl) piperazine-2-carboxamide · ligand · chains A
MG · Magnesium ion · metal · chains A
CL · Chloride ion · ion · 6 copies · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	477	0.67	0.79	56	CL
2	82	0.40	0.78	24	empty
3	80	0.35	0.75	15	empty
4	64	0.30	0.74	16	empty

Compared structures

6SO4 · Fragment RZ132 in complex with MAP kinase p38-alpha · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P47811
Elsewhere: RCSB PDB 6SO4 · PDBe 6SO4 · UniProt P47811

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