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Crystal structure of adenosine deaminase complexed with FR230513

Analyse Crystal structure of adenosine deaminase complexed with FR230513 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1NDY
Type: protein
Length: 349 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenosine deaminase
EC: 3.5.4.4
UniProt: P56658
Ligands: FR3, ZN
Pockets: 3 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adenosine deaminase (EC 3.5.4.4)	protein	349	54% helix, 14% strand	P56658

Ligands and binding sites

FR3 · 1-((1R)-1-(hydroxymethyl)-3-(1-naphthyl)propyl)-1H-imidazole-4-carboxamide · 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	338	0.73	0.85	40	FR3
2	92	0.39	0.77	19	empty
3	64	0.33	0.76	12	empty

Compared structures

1NDY · Crystal Structure of Adenosine Deaminase Complexed with FR230513 · the same entry in another collection · chain A against A, TM-score 1.00
P56658 · AlphaFold monomer V2.0 prediction for adenosine deaminase (P56658) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P56658
Elsewhere: RCSB PDB 1NDY · PDBe 1NDY · UniProt P56658

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