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The structure of the arabidopsis thaliana guanosine deaminase complexed with inosine

Analyse The structure of the arabidopsis thaliana guanosine deaminase complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7DCB
Type: protein
Length: 314 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Guanosine deaminase
EC: 3.5.4.15
UniProt: Q94BU8
Ligands: NOS, ZN
Pockets: 3 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D	Guanosine deaminase (EC 3.5.4.15)	protein	157	43% helix, 18% strand	Q94BU8

Ligands and binding sites

NOS · Inosine · ligand · 2 copies · chains A, D
ZN · Zinc ion · metal · 2 copies · chains A, D

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	109	0.78	0.97	26	NOS
2	134	0.72	0.91	20	NOS
3	68	0.28	0.73	12	empty

Interfaces

1 interface between chains.

A–D · 1622 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

7DCB · The structure of the Arabidopsis thaliana guanosine deaminase complexed with inosine · the same entry in another collection · chain A against A, TM-score 1.00
Q94BU8 · AlphaFold monomer V2.0 prediction for guanosine deaminase (Q94BU8) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q94BU8
Elsewhere: RCSB PDB 7DCB · PDBe 7DCB · UniProt Q94BU8

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