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Crystal structure of arabidopsis adal complexed with gmp

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

PDB: 6J23
Type: protein
Length: 338 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ADENOSINE/AMP deaminase family protein
UniProt: Q8LPL7
Ligands: 5GP, ZN
Pockets: 3 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ADENOSINE/AMP deaminase family protein	protein	338	54% helix, 16% strand	Q8LPL7

Ligands and binding sites

5GP · Guanosine-5'-monophosphate · ligand · chains A
ZN · Zinc ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	136	0.75	0.93	31	5GP
2	65	0.32	0.75	16	empty
3	75	0.29	0.73	13	empty

Compared structures

6J23 · Crystal structure of arabidopsis ADAL complexed with GMP · the same entry in another collection · chain A against A, TM-score 1.00
Q8LPL7 · AlphaFold monomer V2.0 prediction for N6-mamp deaminase (Q8LPL7) · a predicted model of the same protein · 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 Q8LPL7
Elsewhere: RCSB PDB 6J23 · PDBe 6J23 · UniProt Q8LPL7

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