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Actin-fragmin kinase, catalytic domain from physarum polycephalum

Analyse Actin-fragmin kinase, catalytic domain from physarum polycephalum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1CJA
Type: protein
Length: 654 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (actin-fragmin kinase)
UniProt: Q94706
Ligands: AMP
Pockets: 9 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein (actin-fragmin kinase)	protein	327	46% helix, 13% strand	Q94706

Ligands and binding sites

AMP · Adenosine monophosphate · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	378	0.69	0.81	41	AMP
2	363	0.68	0.81	34	AMP
3	181	0.54	0.79	22	empty
4	197	0.54	0.78	24	empty
5	84	0.39	0.78	27	empty

Interfaces

1 interface between chains.

A–B · 387 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

1CJA · Actin-fragmin kinase, catalytic domain from physarum polycephalum · the same entry in another collection · chain B against B, TM-score 1.00

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 Q94706
Elsewhere: RCSB PDB 1CJA · PDBe 1CJA · UniProt Q94706

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