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Crystal structure of a nicotinate nucleotide pyrophosphorylase (TM1645) from thermotoga maritima at 2.50 a resolution

Analyse Crystal structure of a nicotinate nucleotide pyrophosphorylase (TM1645) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1O4U
Type: protein
Length: 531 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Type II quinolic acid phosphoribosyltransferase
UniProt: Q9X1X8
Pockets: 4 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Type II quinolic acid phosphoribosyltransferase	protein	265	43% helix, 22% strand	Q9X1X8
B	Type II quinolic acid phosphoribosyltransferase	protein	266	44% helix, 23% strand	Q9X1X8

Pockets

4 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	943	0.78	0.80	94	empty
2	982	0.75	0.78	81	empty
3	139	0.43	0.75	23	empty
4	54	0.28	0.74	14	empty

Interfaces

1 interface between chains.

A–B · 2067 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

1O4U · Crystal structure of a nicotinate nucleotide pyrophosphorylase (tm1645) from thermotoga… · 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 Q9X1X8
Elsewhere: RCSB PDB 1O4U · PDBe 1O4U · UniProt Q9X1X8

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