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Crystal structure of MAPKAP2

Analyse Crystal structure of MAPKAP2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1KWP
Type: protein
Length: 632 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MAP kinase activated protein kinase 2
EC: 2.7.1.-
UniProt: P49137
Ligands: HG
Pockets: 11 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	MAP kinase activated protein kinase 2 (EC 2.7.1.-)	protein	319	35% helix, 13% strand	P49137
B	MAP kinase activated protein kinase 2 (EC 2.7.1.-)	protein	313	35% helix, 16% strand	P49137

Ligands and binding sites

HG · Mercury (II) ion · metal · 14 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	455	0.59	0.75	46	empty
2	195	0.56	0.79	39	empty
3	136	0.53	0.81	28	HG
4	145	0.52	0.80	25	empty
5	131	0.49	0.79	27	HG

Interfaces

1 interface between chains.

A–B · 432 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

1KWP · Crystal Structure of MAPKAP2 · the same entry in another collection · chain A against A, TM-score 1.00
P49137 · AlphaFold monomer V2.0 prediction for MAP kinase-activated protein kinase 2 (P49137) · a predicted model of the same protein · chain A against A, TM-score 0.88

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P49137
Elsewhere: RCSB PDB 1KWP · PDBe 1KWP · UniProt P49137

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