eF-site ID 1a4l-D PDB Code 1a4l Chain D 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 D:  TPAFNKPKVELHVHLDGAIKPETILYFGKKRGIALPADTV EELRNIIGMDKPLSLPGFLAKFDYYMPVIAGCREAIKRIA YEFVEMKAKEGVVYVEVRYSPHLLANSKVDPMPWNQTEGD VTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRHQPSWSL EVLELCKKYNQKTVVAMDLAGDETIEGSSLFPGHVEAYEG AVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTI EDEALYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRF KNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFK RLNINAAKSSFLPEEEKKELLERLYREYQ Description Functional site 1) chain D residue 1515 type sequence H description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CID 2) chain D residue 1517 type sequence H description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CID 3) chain D residue 1519 type sequence D description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CID 4) chain D residue 1684 type sequence G description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CID 5) chain D residue 1714 type sequence H description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CID 6) chain D residue 1717 type sequence E description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CID 7) chain D residue 1738 type sequence H description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CID 8) chain D residue 1795 type sequence D description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CID 9) chain D residue 1796 type sequence D description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CID 10) chain D residue 1515 type sequence H description BINDING SITE FOR RESIDUE ZN D 1900 source : AC1 11) chain D residue 1517 type sequence H description BINDING SITE FOR RESIDUE ZN D 1900 source : AC1 12) chain D residue 1714 type sequence H description BINDING SITE FOR RESIDUE ZN D 1900 source : AC1 13) chain D residue 1795 type sequence D description BINDING SITE FOR RESIDUE ZN D 1900 source : AC1 14) chain D residue 1517 type sequence H description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 15) chain D residue 1519 type sequence D description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 16) chain D residue 1558 type sequence L description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 17) chain D residue 1561 type sequence F description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 18) chain D residue 1565 type sequence F description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 19) chain D residue 1602 type sequence Y description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 20) chain D residue 1603 type sequence S description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 21) chain D residue 1606 type sequence L description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 22) chain D residue 1655 type sequence M description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 23) chain D residue 1683 type sequence A description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 24) chain D residue 1684 type sequence G description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 25) chain D residue 1714 type sequence H description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 26) chain D residue 1717 type sequence E description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 27) chain D residue 1738 type sequence H description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 28) chain D residue 1795 type sequence D description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 29) chain D residue 1796 type sequence D description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 30) chain D residue 1515 type catalytic sequence H description 376 source MCSA : MCSA4 31) chain D residue 1517 type catalytic sequence H description 376 source MCSA : MCSA4 32) chain D residue 1714 type catalytic sequence H description 376 source MCSA : MCSA4 33) chain D residue 1717 type catalytic sequence E description 376 source MCSA : MCSA4 34) chain D residue 1738 type catalytic sequence H description 376 source MCSA : MCSA4 35) chain D residue 1795 type catalytic sequence D description 376 source MCSA : MCSA4 36) chain D residue 1515 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 37) chain D residue 1517 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 38) chain D residue 1714 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 D residue 1795 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 40) chain D residue 1519 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 41) chain D residue 1684 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 42) chain D residue 1554 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00813 source Swiss-Prot : SWS_FT_FI8 43) chain D residue 1732 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00813 source Swiss-Prot : SWS_FT_FI8 44) chain D residue 1796 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 D residue 1717 type ACT_SITE sequence E description Proton donor => ECO:0000305|PubMed:8634299, ECO:0000305|PubMed:9622483 source Swiss-Prot : SWS_FT_FI1 46) chain D residue 1558 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 D residue 1562 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 48) chain D residue 1738 type SITE sequence H description Important for catalytic activity => ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483 source Swiss-Prot : SWS_FT_FI7

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