Research workbench

MAPK13, active form

Analyse MAPK13, active form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4MYG
Type: protein
Length: 674 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mitogen-activated protein kinase 13
EC: 2.7.11.24
UniProt: O15264
Pockets: 9 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Mitogen-activated protein kinase 13 (EC 2.7.11.24)	protein	337	36% helix, 13% strand	O15264

Pockets

9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	530	0.71	0.80	51	empty
2	520	0.69	0.79	51	empty
3	378	0.68	0.81	48	empty
4	382	0.67	0.81	39	empty
5	503	0.67	0.78	53	empty

Interfaces

1 interface between chains.

A–B · 857 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (phosphorylation).

Compared structures

4MYG · MAPK13, active form · the same entry in another collection · chain A against A, TM-score 1.00
O15264 · AlphaFold monomer V2.0 prediction for mitogen-activated protein kinase 13 (O15264) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 O15264
Elsewhere: RCSB PDB 4MYG · PDBe 4MYG · UniProt O15264

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