MolNFT v1 · #164289 · protein

Crystal structure of LICM2

6ST5: “Crystal structure of LICM2”. X-ray diffraction, 3 ligands (ANP, ZN, MG), 13 pockets (best druggability 0.71). MolNFT v1 #164289 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6ST5
Type: protein
Length: 913 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: LICM2
UniProt: E9MWH4
Ligands: ANP, ZN, MG
Pockets: 13 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	LICM2	protein	913	53% helix, 8% strand	E9MWH4

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
ZN · Zinc ion · metal · chains A
MG · Magnesium ion · metal · chains A
GOL · Glycerol · additive · 8 copies · chains A

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

Pockets

13 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	597	0.71	0.79	56	ANP, MG
2	61	0.71	0.97	17	GOL
3	191	0.63	0.84	29	empty
4	175	0.55	0.80	38	empty
5	137	0.50	0.79	20	empty

Modifications

Observed in the structure: 19 modified (engineered).

Compared structures

6ST5 · crystal structure of LicM2 · 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 E9MWH4
Elsewhere: RCSB PDB 6ST5 · PDBe 6ST5 · UniProt E9MWH4

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