eF-site ID 1v79-A PDB Code 1v79 Chain A click to enlarge Title Crystal structures of adenosine deaminase complexed with potent inhibitors Classification HYDROLASE Compound Adenosine deaminase Source ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus; Sequence A:  TPAFDKPKVELHVHLDGAIKPETILYYGKRRGIALPADTP EELQNIIGMDKPLTLPDFLAKFDYYMPAIAGCRDAIKRIA YEFVEMKAKDGVVYVEVRYSPHLLANSKVEPIPWNQAEGD LTPDEVVSLVNQGLQEGERDFGVKVRSILCCMRHQPSWSS EVVELCKKYREQTVVAIDLAGDETIEGSSLFPGHVQAYAE AVKSGVHRTVHAGEVGSANVVKEAVDTLKTERLGHGYHTL EDTTLYNRLRQENMHFEICPWSSYLTGAWKPDTEHAVIRF KNDQVNYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFK RLNINAAKSSFLPEDEKKELLDLLYKAYR Description Functional site 1) chain A residue 15 type sequence H description BINDING SITE FOR RESIDUE ZN A 400 source : AC1 2) chain A residue 17 type sequence H description BINDING SITE FOR RESIDUE ZN A 400 source : AC1 3) chain A residue 214 type sequence H description BINDING SITE FOR RESIDUE ZN A 400 source : AC1 4) chain A residue 295 type sequence D description BINDING SITE FOR RESIDUE ZN A 400 source : AC1 5) chain A residue 17 type sequence H description BINDING SITE FOR RESIDUE FR7 A 1001 source : AC2 6) chain A residue 19 type sequence D description BINDING SITE FOR RESIDUE FR7 A 1001 source : AC2 7) chain A residue 62 type sequence L description BINDING SITE FOR RESIDUE FR7 A 1001 source : AC2 8) chain A residue 65 type sequence F description BINDING SITE FOR RESIDUE FR7 A 1001 source : AC2 9) chain A residue 102 type sequence Y description BINDING SITE FOR RESIDUE FR7 A 1001 source : AC2 10) chain A residue 103 type sequence S description BINDING SITE FOR RESIDUE FR7 A 1001 source : AC2 11) chain A residue 106 type sequence L description BINDING SITE FOR RESIDUE FR7 A 1001 source : AC2 12) chain A residue 117 type sequence W description BINDING SITE FOR RESIDUE FR7 A 1001 source : AC2 13) chain A residue 183 type sequence A description BINDING SITE FOR RESIDUE FR7 A 1001 source : AC2 14) chain A residue 185 type sequence D description BINDING SITE FOR RESIDUE FR7 A 1001 source : AC2 15) chain A residue 296 type sequence D description BINDING SITE FOR RESIDUE FR7 A 1001 source : AC2 16) chain A residue 55 type MOD_RES sequence P description N6-acetyllysine => ECO:0000250|UniProtKB:P00813 source Swiss-Prot : SWS_FT_FI9 17) chain A residue 233 type MOD_RES sequence T description N6-acetyllysine => ECO:0000250|UniProtKB:P00813 source Swiss-Prot : SWS_FT_FI9 18) chain A residue 218 type ACT_SITE sequence V description Proton donor => ECO:0000250|UniProtKB:P03958 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 16 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL source Swiss-Prot : SWS_FT_FI2 20) chain A residue 18 type BINDING sequence L description BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL source Swiss-Prot : SWS_FT_FI2 21) chain A residue 215 type BINDING sequence A description BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL source Swiss-Prot : SWS_FT_FI2 22) chain A residue 296 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL source Swiss-Prot : SWS_FT_FI2 23) chain A residue 63 type SITE sequence A description Important for interaction with adenosine receptors and increasing their affinity for agonists => ECO:0000250|UniProtKB:P00813 source Swiss-Prot : SWS_FT_FI6 24) chain A residue 59 type SITE sequence P description Important for interaction with adenosine receptors and increasing their affinity for agonists => ECO:0000250|UniProtKB:P00813 source Swiss-Prot : SWS_FT_FI6 25) chain A residue 239 type SITE sequence G description Important for catalytic activity => ECO:0000250|UniProtKB:P03958 source Swiss-Prot : SWS_FT_FI7 26) chain A residue 291-297 type prosite sequence SLNTDDP description A_DEAMINASE Adenosine and AMP deaminase signature. SLNTDDP source prosite : PS00485 27) chain A residue 20 type BINDING sequence G description BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL source Swiss-Prot : SWS_FT_FI3 28) chain A residue 185 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:16060665, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1WXY source Swiss-Prot : SWS_FT_FI4 29) chain A residue 297 type BINDING sequence P description BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL source Swiss-Prot : SWS_FT_FI5

Display surface Download Links