MolNFT v1 · #181004 · protein

High-resolution crystal structure of a LIPIN/PAH phosphatidic acid phosphatase

7LHK · Nuclear elongation and deformation protein: “High-resolution crystal structure of a LIPIN/PAH phosphatidic acid phosphatase”. X-ray diffraction, 4 pockets (best druggability 0.78). MolNFT v1 #181004 on GenesisL1: 3D structure…

PDB: 7LHK
Type: protein
Length: 592 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nuclear elongation and deformation protein
UniProt: I7MFJ3
Pockets: 4 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nuclear elongation and deformation protein	protein	294	28% helix, 31% strand	I7MFJ3
B	Nuclear elongation and deformation protein	protein	298	27% helix, 35% strand	I7MFJ3

Ligands and binding sites

CAC · Cacodylate ion · additive · 2 copies · chains A, B

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

Pockets

4 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	1064	0.78	0.80	87	empty
2	284	0.63	0.80	46	empty
3	83	0.60	0.88	21	empty
4	63	0.43	0.82	18	CAC

Interfaces

1 interface between chains.

A–B · 703 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

7LHK · High-Resolution Crystal Structure of a Lipin/Pah Phosphatidic Acid Phosphatase · 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 I7MFJ3
Elsewhere: RCSB PDB 7LHK · PDBe 7LHK · UniProt I7MFJ3

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