MolNFT v1 · #48715 · protein

Crystal structure of the bordetella bronchiseptica enzyme wbmf in complex with NAD+ and udp

2Q1T · Putative nucleotide sugar epimerase/ dehydratase: “Crystal structure of the bordetella bronchiseptica enzyme wbmf in complex with NAD+ and udp”. X-ray diffraction, 2 ligands (NAD, UDP), 1 pocket (best druggability 0.75). MolNFT v1…

PDB: 2Q1T
Type: protein
Length: 332 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative nucleotide sugar epimerase/ dehydratase
UniProt: O87989
Ligands: NAD, UDP
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative nucleotide sugar epimerase/ dehydratase	protein	332	43% helix, 12% strand	O87989

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
UDP · Uridine-5'-diphosphate · ligand · 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	728	0.75	0.80	83	NAD, UDP

Compared structures

2Q1T · Crystal structure of the Bordetella bronchiseptica enzyme WbmF in complex with NAD+ and… · 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 O87989
Elsewhere: RCSB PDB 2Q1T · PDBe 2Q1T · UniProt O87989

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