Crystal structure of the E. coli pyrimidine nucleoside hydrolase YeiK in complex with inosine

Structural basis for substrate specificity in group I nucleoside hydrolases

Crystal structure to 1.7 a of the Escherichia coli pyrimidine nucleoside hydrolase YeiK, a novel candidate for cancer gene therapy

Trypanosomal nucleoside hydrolase. A novel mechanism from the structure with a transition-state inhibitor

Pyrimidine-specific ribonucleoside hydrolase rihB

MGSSHHHHHHSSGLVPRGSHMEKRKIILDCDPGHDDAIAIMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEIN
VPVYAGMPQPIMRQQIVADNIHGDTGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAI
LPKIREIVLMGGAYGTGNFTPSAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIM
NFTLKTQFENYGLAGGPVHDATCIGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWG
LVEECVRGYIKTH

0.1M Tris-HCl, 0.2M NaCl, 24% PEG 4000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

E.coli pyrimidine-specific nucleoside hydrolase YeiK bound to glycerol

Protozoan non-specific (IU) nucleoside hydrolase in complex with transition state inhibitor

THE AUTHORS FEEL THAT THE CONFLICT REPRESENTS A MUTATION IN THE DEPOSITED SEQUENCE.

Open (alpha, beta) structure, NH-fold, enzyme-substrate complex, protein-nucleoside complex, Glycosidase, Hydrolase, Metal-binding

MEKRKIILDCDPGHDDAIAIMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEINVPVYAGMPQPIMRQQIVADN
IHGETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGTGNFT
PSAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTQFENYGLAGGPVHD
ATCIGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVEECVRGYIKTH