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Crystal structure of AMP nucleosidase from salmonella typhimurium LT2

Analyse Crystal structure of AMP nucleosidase from salmonella typhimurium LT2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2GUW
Type: protein
Length: 1,223 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: AMP nucleosidase
EC: 3.2.2.4
UniProt: Q8ZNS0
Pockets: 19 · best druggability 0.87

Structure

x-ray diffraction · 3 distinct chains · 42% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	AMP nucleosidase (EC 3.2.2.4)	protein	411	40% helix, 18% strand	Q8ZNS0
B	AMP nucleosidase (EC 3.2.2.4)	protein	418	43% helix, 20% strand	Q8ZNS0
C	AMP nucleosidase (EC 3.2.2.4)	protein	394	41% helix, 21% strand	Q8ZNS0

Pockets

19 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1153	0.87	0.88	134	empty
2	470	0.75	0.83	41	empty
3	656	0.71	0.78	75	empty
4	71	0.70	0.95	16	empty
5	432	0.69	0.80	52	empty

Interfaces

2 interfaces between chains.

A–B · 2767 Å² buried · 26 hydrogen bonds · protein-protein
B–C · 888 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

2GUW · Crystal structure of AMP Nucleosidase from Salmonella typhimurium LT2 · 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 Q8ZNS0
Elsewhere: RCSB PDB 2GUW · PDBe 2GUW · UniProt Q8ZNS0

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