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The crystal structure of adenine deaminase (AAUR1117) from arthrobacter aurescens

Analyse The crystal structure of adenine deaminase (AAUR1117) from arthrobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3RYS
Type: protein
Length: 662 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenosine deaminase 1
EC: 3.5.4.4
UniProt: A1R3U3
Ligands: ADE, ZN
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 54% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adenosine deaminase 1 (EC 3.5.4.4)	protein	335	54% helix, 13% strand	A1R3U3
B	Adenosine deaminase 1 (EC 3.5.4.4)	protein	327	54% helix, 14% strand	A1R3U3

Ligands and binding sites

ADE · Adenine · ligand · 2 copies · chains A, B
ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	746	0.71	0.77	73	empty

Interfaces

1 interface between chains.

A–B · 549 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3RYS · The crystal structure of adenine deaminase (AAur1117) from Arthrobacter aurescens · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A1R3U3
Elsewhere: RCSB PDB 3RYS · PDBe 3RYS · UniProt A1R3U3

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