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Crystal structure of a putative ntp pyrophosphohydrolase (EXIG_1061) from exiguobacterium sp. 255-15 at 1.78 a resolution

Analyse Crystal structure of a putative ntp pyrophosphohydrolase (EXIG_1061) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NL9
Type: protein
Length: 169 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative ntp pyrophosphohydrolase
UniProt: B1YMF4
Pockets: 1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 64% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative ntp pyrophosphohydrolase	protein	169	64% helix, 1% strand	B1YMF4

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 2 copies · chains A

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	840	0.67	0.73	55	EDO

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

3NL9 · Crystal structure of a putative NTP pyrophosphohydrolase (Exig_1061) from EXIGUOBACTERIUM… · 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 B1YMF4
Elsewhere: RCSB PDB 3NL9 · PDBe 3NL9 · UniProt B1YMF4

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