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Crystal structure of E. COLI MTA/ADOHCY nucleosidase

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

PDB: 1JYS
Type: protein
Length: 452 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MTA/SAH nucleosidase
EC: 3.2.2.9
UniProt: P24247
Ligands: ADE
Pockets: 5 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	MTA/SAH nucleosidase (EC 3.2.2.9)	protein	226	37% helix, 33% strand	P24247

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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	294	0.64	0.80	33	ADE
2	277	0.62	0.80	33	empty
3	281	0.58	0.78	34	ADE
4	86	0.36	0.75	23	empty
5	83	0.34	0.74	18	empty

Interfaces

1 interface between chains.

A–B · 1270 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

1JYS · Crystal Structure of E. coli MTA/AdoHcy Nucleosidase · the same entry in another collection · 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 P24247
Elsewhere: RCSB PDB 1JYS · PDBe 1JYS · UniProt P24247

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