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Catalytic and ubiqutin-associated domains of MARK2/PAR-1: inactive double mutant with selenomethionine

Analyse Catalytic and ubiqutin-associated domains of MARK2/PAR-1: inactive double… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Y8G
Type: protein
Length: 604 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MAP/MICROTUBULE affinity-regulating kinase 2
EC: 2.7.1.37
Pockets: 4 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	MAP/MICROTUBULE affinity-regulating kinase 2 (EC 2.7.1.37)	protein	302	44% helix, 15% strand	—
B	MAP/MICROTUBULE affinity-regulating kinase 2 (EC 2.7.1.37)	protein	302	42% helix, 16% strand	—

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1020	0.79	0.81	97	empty
2	1176	0.76	0.78	87	empty
3	193	0.50	0.77	27	empty
4	213	0.49	0.75	30	empty

Interfaces

1 interface between chains.

A–B · 1448 Å² buried · 24 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 modified, 1 disulfide (engineered, disulfide).

Compared structures

1Y8G · Catalytic and ubiqutin-associated domains of MARK2/PAR-1: Inactive double mutant with… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 1Y8G · PDBe 1Y8G

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