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A crucial role of CYS218 in the stabilization of an unprecedented auto-inhibition form of MAP2K7

Analyse A crucial role of CYS218 in the stabilization of an unprecedented… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5B2K
Type: protein
Length: 264 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dual specificity mitogen-activated protein kinase kinase 7
EC: 2.7.12.2
UniProt: O14733
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dual specificity mitogen-activated protein kinase kinase 7 (EC 2.7.12.2)	protein	264	36% helix, 15% strand	O14733

Pockets

3 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	357	0.68	0.81	46	empty
2	53	0.29	0.75	13	empty
3	53	0.26	0.73	15	empty

Compared structures

5B2K · A crucial role of Cys218 in the stabilization of an unprecedented auto-inhibition form of… · the same entry in another collection · chain A against A, TM-score 1.00
O14733 · AlphaFold monomer V2.0 prediction for dual specificity mitogen- activated protein kinase… · a predicted model of the same protein · chain A against A, TM-score 0.94

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 O14733
Elsewhere: RCSB PDB 5B2K · PDBe 5B2K · UniProt O14733

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