Crystal structure of human carbonic anhydrase II at 1.95 A resolution in complex with 667-coumate, a novel anti-cancer agent.
Lloyd
Matthew D
MD
Medicinal Chemistry, Department of Pharmacy and Pharmacology, University of Bath, Claverton Down, Bath BA2 7AY, UK. M.D.Lloyd@bath.ac.uk
Pederick
Richard L
RL
Natesh
Ramanathan
R
Woo
L W Lawrence
LW
Purohit
Atul
A
Reed
Michael J
MJ
Acharya
K Ravi
KR
Potter
Barry V L
BV
D000970:Antineoplastic Agents / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D024402:Carbonic Anhydrase II / Q000737:chemistry* / Q000378:metabolism*; D003374:Coumarins / Q000737:chemistry* / Q000378:metabolism*; D018360:Crystallography, X-Ray; D006207:Half-Life; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D009584:Nitrogen / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013449:Sulfonamides / Q000737:chemistry* / Q000378:metabolism*; D013451:Sulfonic Acids; D015032:Zinc / Q000737:chemistry / Q000378:metabolism
D000970:Antineoplastic Agents; D003374:Coumarins; D013449:Sulfonamides; D013451:Sulfonic Acids; C520511:irosustat; D024402:Carbonic Anhydrase II; D015032:Zinc; D009584:Nitrogen