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Crystal structure of the MTA/SAH nucleosidase

Analyse Crystal structure of the MTA/SAH nucleosidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3BSF
Type: protein
Length: 488 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: AT4G34840
UniProt: Q7XA67
Ligands: ADE
Pockets: 4 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	AT4G34840	protein	244	32% helix, 27% strand	Q7XA67

Ligands and binding sites

ADE · Adenine · ligand · 2 copies · chains A, B

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

Pockets

4 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	187	0.78	0.93	32	ADE
2	324	0.74	0.86	34	ADE
3	56	0.59	0.91	20	empty
4	58	0.57	0.89	20	empty

Interfaces

1 interface between chains.

A–B · 2056 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

3BSF · Crystal Structure of the MTA/SAH nucleosidase · the same entry in another collection · chain A against A, TM-score 1.00
Q7XA67 · AlphaFold monomer V2.0 prediction for 5'-METHYLTHIOADENOSINE/S-adenosylhomocysteine… · a predicted model of the same protein · chain A against A, TM-score 0.98

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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 Q7XA67
Elsewhere: RCSB PDB 3BSF · PDBe 3BSF · UniProt Q7XA67

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