Research workbench

Crystal structure of PF11_0147

Analyse Crystal structure of PF11_0147 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NIE
Type: protein
Length: 736 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MAP2 kinase
UniProt: Q9GR08
Ligands: ANP
Pockets: 9 · best druggability 0.86

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	MAP2 kinase	protein	369	39% helix, 14% strand	Q9GR08
B	MAP2 kinase	protein	367	36% helix, 13% strand	Q9GR08

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1169	0.86	0.87	108	ANP
2	162	0.56	0.81	24	empty
3	178	0.52	0.78	36	empty
4	84	0.48	0.82	17	empty
5	66	0.34	0.77	14	empty

Interfaces

1 interface between chains.

A–B · 1697 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

3NIE · Crystal Structure of PF11_0147 · the same entry in another collection · chain A against A, 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 Q9GR08
Elsewhere: RCSB PDB 3NIE · PDBe 3NIE · UniProt Q9GR08

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.