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Crystal structure of ADP-ribosyltransferase vis in complex with NAD

Analyse Crystal structure of ADP-ribosyltransferase vis in complex with NAD in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4XZJ
Type: protein
Length: 222 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative NAD(+)--arginine ADP-ribosyltransferase vis
EC: 2.4.2.31
UniProt: A3UNN4
Ligands: NAD
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative NAD(+)--arginine ADP-ribosyltransferase vis (EC 2.4.2.31)	protein	222	38% helix, 27% strand	A3UNN4

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	391	0.67	0.80	35	NAD
2	85	0.38	0.76	17	empty

Compared structures

4XZJ · Crystal structure of ADP-ribosyltransferase Vis in complex with NAD · the same entry in another collection · chain A against A, TM-score 1.00
A3UNN4 · AlphaFold monomer V2.0 prediction for putative NAD(+)--arginine ADP- ribosyltransferase… · a predicted model of the same protein · chain A against A, TM-score 0.98

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 A3UNN4
Elsewhere: RCSB PDB 4XZJ · PDBe 4XZJ · UniProt A3UNN4

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