MolNFT v1 · #99032 · protein

Bacterial effector NLEH1 kinase domain with amppnp and MG2+

4LRJ: “Bacterial effector NLEH1 kinase domain with amppnp and MG2+”. X-ray diffraction, 2 ligands (ANP, MG), 3 pockets (best druggability 0.59). MolNFT v1 #99032 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4LRJ
Type: protein
Length: 319 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Effector NLEH1
EC: 2.7.11.1
UniProt: Q8X831
Ligands: ANP, MG
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Effector NLEH1 (EC 2.7.11.1)	protein	160	31% helix, 27% strand	Q8X831
B	Effector NLEH1 (EC 2.7.11.1)	protein	159	31% helix, 27% strand	Q8X831

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 4 copies · chains A, B

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

Pockets

3 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	349	0.59	0.77	35	ANP, MG
2	227	0.54	0.78	28	ANP, MG
3	285	0.51	0.74	33	empty

Interfaces

1 interface between chains.

A–B · 191 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

4LRJ · Bacterial Effector NleH1 Kinase Domain with AMPPNP and Mg2+ · 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 Q8X831
Elsewhere: RCSB PDB 4LRJ · PDBe 4LRJ · UniProt Q8X831

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