Research workbench

APO MAP4K4 T181E Phosphomimetic Mutant

Analyse APO MAP4K4 T181E Phosphomimetic Mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4U3Z
Type: protein
Length: 576 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.09
Source: Homo sapiens
Molecule: Mitogen-activated protein kinase kinase kinase kinase 4
EC: 2.7.11.1
UniProt: O95819
Ligands: NA
Pockets: 7 · best druggability 0.83

Structure

x-ray diffraction · resolution 2.09 · 2 distinct chains · 38% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Mitogen-activated protein kinase kinase kinase kinase 4 (EC 2.7.11.1)	protein	294	37% helix, 17% strand	O95819
A	Mitogen-activated protein kinase kinase kinase kinase 4 (EC 2.7.11.1)	protein	282	39% helix, 16% strand	O95819

Ligands and binding sites

NA · Sodium ion · metal · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A

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

Pockets

7 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	838	0.83	0.85	74	empty
2	540	0.77	0.84	54	empty
3	116	0.58	0.85	27	empty
4	50	0.44	0.84	15	empty
5	71	0.37	0.77	18	empty

Interfaces

1 interface between chains.

B–A · 1415 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

4U3Z · Apo MAP4K4 T181E phosphomimetic mutant · the same entry in another collection · chain A against A, TM-score 1.00
O95819 · AlphaFold monomer V2.0 prediction for mitogen-activated protein kinase kinase kinase… · a predicted model of the same protein · chain A against A, TM-score 0.90

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 O95819
Elsewhere: RCSB PDB 4U3Z · PDBe 4U3Z · UniProt O95819

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