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Crystal structure of the apo ERK5 kinase domain

Analyse Crystal structure of the apo ERK5 kinase domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4IC8
Type: protein
Length: 661 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mitogen-activated protein kinase 7
EC: 2.7.11.24
UniProt: Q13164
Pockets: 8 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 7 (EC 2.7.11.24)	protein	325	33% helix, 11% strand	Q13164
B	Mitogen-activated protein kinase 7 (EC 2.7.11.24)	protein	336	32% helix, 12% strand	Q13164

Pockets

8 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	821	0.73	0.78	77	empty
2	409	0.68	0.80	40	empty
3	128	0.61	0.85	28	empty
4	128	0.49	0.79	27	empty
5	111	0.49	0.80	23	empty

Interfaces

1 interface between chains.

A–B · 344 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

4IC8 · Crystal structure of the apo ERK5 kinase domain · the same entry in another collection · chain A against A, TM-score 1.00
Q13164 · AlphaFold monomer V2.0 prediction for mitogen-activated protein kinase 7 (Q13164) · a predicted model of the same protein · chain B against A, TM-score 0.91

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 Q13164
Elsewhere: RCSB PDB 4IC8 · PDBe 4IC8 · UniProt Q13164

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