eF-site ID 1a4l-A PDB Code 1a4l Chain A click to enlarge Title ADA STRUCTURE COMPLEXED WITH DEOXYCOFORMYCIN AT PH 7.0 Classification HYDROLASE Compound ADENOSINE DEAMINASE Source Mus musculus (Mouse) (ADA_MOUSE) Sequence A:  TPAFNKPKVELHVHLDGAIKPETILYFGKKRGIALPADTV EELRNIIGMDKPLSLPGFLAKFDYYMPVIAGCREAIKRIA YEFVEMKAKEGVVYVEVRYSPHLLANSKVDPMPWNQTEGD VTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRHQPSWSL EVLELCKKYNQKTVVAMDLAGDETIEGSSLFPGHVEAYEG AVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTI EDEALYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRF KNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFK RLNINAAKSSFLPEEEKKELLERLYREYQ Description Functional site 1) chain A residue 15 type sequence H description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CIA 2) chain A residue 17 type sequence H description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CIA 3) chain A residue 19 type sequence D description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CIA 4) chain A residue 184 type sequence G description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CIA 5) chain A residue 214 type sequence H description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CIA 6) chain A residue 217 type sequence E description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CIA 7) chain A residue 238 type sequence H description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CIA 8) chain A residue 295 type sequence D description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CIA 9) chain A residue 296 type sequence D description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CIA 10) chain A residue 15 type sequence H description BINDING SITE FOR RESIDUE ZN A 400 source : AC4 11) chain A residue 17 type sequence H description BINDING SITE FOR RESIDUE ZN A 400 source : AC4 12) chain A residue 214 type sequence H description BINDING SITE FOR RESIDUE ZN A 400 source : AC4 13) chain A residue 295 type sequence D description BINDING SITE FOR RESIDUE ZN A 400 source : AC4 14) chain A residue 15 type sequence H description BINDING SITE FOR RESIDUE DCF A 353 source : AC5 15) chain A residue 17 type sequence H description BINDING SITE FOR RESIDUE DCF A 353 source : AC5 16) chain A residue 19 type sequence D description BINDING SITE FOR RESIDUE DCF A 353 source : AC5 17) chain A residue 58 type sequence L description BINDING SITE FOR RESIDUE DCF A 353 source : AC5 18) chain A residue 61 type sequence F description BINDING SITE FOR RESIDUE DCF A 353 source : AC5 19) chain A residue 65 type sequence F description BINDING SITE FOR RESIDUE DCF A 353 source : AC5 20) chain A residue 103 type sequence S description BINDING SITE FOR RESIDUE DCF A 353 source : AC5 21) chain A residue 106 type sequence L description BINDING SITE FOR RESIDUE DCF A 353 source : AC5 22) chain A residue 155 type sequence M description BINDING SITE FOR RESIDUE DCF A 353 source : AC5 23) chain A residue 183 type sequence A description BINDING SITE FOR RESIDUE DCF A 353 source : AC5 24) chain A residue 184 type sequence G description BINDING SITE FOR RESIDUE DCF A 353 source : AC5 25) chain A residue 214 type sequence H description BINDING SITE FOR RESIDUE DCF A 353 source : AC5 26) chain A residue 217 type sequence E description BINDING SITE FOR RESIDUE DCF A 353 source : AC5 27) chain A residue 238 type sequence H description BINDING SITE FOR RESIDUE DCF A 353 source : AC5 28) chain A residue 295 type sequence D description BINDING SITE FOR RESIDUE DCF A 353 source : AC5 29) chain A residue 296 type sequence D description BINDING SITE FOR RESIDUE DCF A 353 source : AC5 30) chain A residue 15 type catalytic sequence H description 376 source MCSA : MCSA1 31) chain A residue 17 type catalytic sequence H description 376 source MCSA : MCSA1 32) chain A residue 214 type catalytic sequence H description 376 source MCSA : MCSA1 33) chain A residue 217 type catalytic sequence E description 376 source MCSA : MCSA1 34) chain A residue 238 type catalytic sequence H description 376 source MCSA : MCSA1 35) chain A residue 295 type catalytic sequence D description 376 source MCSA : MCSA1 36) chain A residue 291-297 type prosite sequence SLNTDDP description A_DEAMINASE Adenosine and AMP deaminase signature. SLNTDDP source prosite : PS00485 37) chain A residue 217 type ACT_SITE sequence E description Proton donor => ECO:0000305|PubMed:8634299, ECO:0000305|PubMed:9622483 source Swiss-Prot : SWS_FT_FI1 38) chain A residue 15 type BINDING sequence H description BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4L, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1FKX, ECO:0007744|PDB:1UIO, ECO:0007744|PDB:1UIP, ECO:0007744|PDB:2ADA source Swiss-Prot : SWS_FT_FI2 39) chain A residue 17 type BINDING sequence H description BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4L, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1FKX, ECO:0007744|PDB:1UIO, ECO:0007744|PDB:1UIP, ECO:0007744|PDB:2ADA source Swiss-Prot : SWS_FT_FI2 40) chain A residue 214 type BINDING sequence H description BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4L, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1FKX, ECO:0007744|PDB:1UIO, ECO:0007744|PDB:1UIP, ECO:0007744|PDB:2ADA source Swiss-Prot : SWS_FT_FI2 41) chain A residue 295 type BINDING sequence D description BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4L, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1FKX, ECO:0007744|PDB:1UIO, ECO:0007744|PDB:1UIP, ECO:0007744|PDB:2ADA source Swiss-Prot : SWS_FT_FI2 42) chain A residue 19 type BINDING sequence D description BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4L, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1FKX source Swiss-Prot : SWS_FT_FI3 43) chain A residue 184 type BINDING sequence G description BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKX, ECO:0007744|PDB:1UIO, ECO:0007744|PDB:1UIP, ECO:0007744|PDB:2ADA source Swiss-Prot : SWS_FT_FI4 44) chain A residue 296 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1UIP source Swiss-Prot : SWS_FT_FI5 45) chain A residue 58 type SITE sequence L description Important for interaction with adenosine receptors and increasing their affinity for agonists => ECO:0000250|UniProtKB:P00813 source Swiss-Prot : SWS_FT_FI6 46) chain A residue 62 type SITE sequence L description Important for interaction with adenosine receptors and increasing their affinity for agonists => ECO:0000250|UniProtKB:P00813 source Swiss-Prot : SWS_FT_FI6 47) chain A residue 238 type SITE sequence H description Important for catalytic activity => ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483 source Swiss-Prot : SWS_FT_FI7 48) chain A residue 54 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00813 source Swiss-Prot : SWS_FT_FI8 49) chain A residue 232 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00813 source Swiss-Prot : SWS_FT_FI8

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