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Crystal structure of sus scrofa quinolinate phosphoribosyltransferase in complex with nicotinate mononucleotide

Analyse Crystal structure of sus scrofa quinolinate phosphoribosyltransferase in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4I9A
Type: protein
Length: 576 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Quinolinate phosphoribosyltransferase
EC: 2.4.2.19
Ligands: NCN
Pockets: 5 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Quinolinate phosphoribosyltransferase (EC 2.4.2.19)	protein	288	45% helix, 19% strand	—

Ligands and binding sites

NCN · Nicotinate mononucleotide · 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	102	0.74	0.95	21	empty
2	348	0.72	0.84	38	NCN
3	354	0.70	0.83	40	NCN
4	225	0.48	0.74	27	empty
5	80	0.31	0.73	17	empty

Interfaces

1 interface between chains.

A–B · 2539 Å² buried · 36 hydrogen bonds · protein-protein

Compared structures

4I9A · Crystal Structure of Sus scrofa Quinolinate Phosphoribosyltransferase in Complex with… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 4I9A · PDBe 4I9A

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