eF-site ID 1a4l-BD PDB Code 1a4l Chain B, 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 B:  TPAFNKPKVELHVHLDGAIKPETILYFGKKRGIALPADTV EELRNIIGMDKPLSLPGFLAKFDYYMPVIAGCREAIKRIA YEFVEMKAKEGVVYVEVRYSPHLLANSKVDPMPWNQTEGD VTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRHQPSWSL EVLELCKKYNQKTVVAMDLAGDETIEGSSLFPGHVEAYEG AVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTI EDEALYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRF KNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFK RLNINAAKSSFLPEEEKKELLERLYREYQ D:  TPAFNKPKVELHVHLDGAIKPETILYFGKKRGIALPADTV EELRNIIGMDKPLSLPGFLAKFDYYMPVIAGCREAIKRIA YEFVEMKAKEGVVYVEVRYSPHLLANSKVDPMPWNQTEGD VTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRHQPSWSL EVLELCKKYNQKTVVAMDLAGDETIEGSSLFPGHVEAYEG AVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTI EDEALYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRF KNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFK RLNINAAKSSFLPEEEKKELLERLYREYQ Description Functional site 1) chain B residue 515 type sequence H description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CIB 2) chain B residue 517 type sequence H description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CIB 3) chain B residue 519 type sequence D description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CIB 4) chain B residue 684 type sequence G description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CIB 5) chain B residue 714 type sequence H description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CIB 6) chain B residue 717 type sequence E description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CIB 7) chain B residue 738 type sequence H description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CIB 8) chain B residue 795 type sequence D description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CIB 9) chain B residue 796 type sequence D description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CIB 10) chain D residue 1515 type sequence H description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CID 11) chain D residue 1517 type sequence H description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CID 12) chain D residue 1519 type sequence D description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CID 13) chain D residue 1684 type sequence G description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CID 14) chain D residue 1714 type sequence H description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CID 15) chain D residue 1717 type sequence E description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CID 16) chain D residue 1738 type sequence H description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CID 17) chain D residue 1795 type sequence D description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CID 18) chain D residue 1796 type sequence D description THE SITE BINDS ADENOSINE AND CONVERT IT TO INOSINE AND AMMONIAGENE. source : CID 19) chain D residue 1515 type sequence H description BINDING SITE FOR RESIDUE ZN D 1900 source : AC1 20) chain D residue 1517 type sequence H description BINDING SITE FOR RESIDUE ZN D 1900 source : AC1 21) chain D residue 1714 type sequence H description BINDING SITE FOR RESIDUE ZN D 1900 source : AC1 22) chain D residue 1795 type sequence D description BINDING SITE FOR RESIDUE ZN D 1900 source : AC1 23) chain B residue 515 type sequence H description BINDING SITE FOR RESIDUE ZN B 900 source : AC3 24) chain B residue 517 type sequence H description BINDING SITE FOR RESIDUE ZN B 900 source : AC3 25) chain B residue 714 type sequence H description BINDING SITE FOR RESIDUE ZN B 900 source : AC3 26) chain B residue 795 type sequence D description BINDING SITE FOR RESIDUE ZN B 900 source : AC3 27) chain B residue 517 type sequence H description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 28) chain B residue 519 type sequence D description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 29) chain B residue 558 type sequence L description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 30) chain B residue 561 type sequence F description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 31) chain B residue 562 type sequence L description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 32) chain B residue 565 type sequence F description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 33) chain B residue 602 type sequence Y description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 34) chain B residue 603 type sequence S description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 35) chain B residue 606 type sequence L description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 36) chain B residue 655 type sequence M description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 37) chain B residue 683 type sequence A description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 38) chain B residue 684 type sequence G description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 39) chain B residue 714 type sequence H description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 40) chain B residue 717 type sequence E description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 41) chain B residue 738 type sequence H description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 42) chain B residue 795 type sequence D description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 43) chain B residue 796 type sequence D description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 44) chain D residue 1517 type sequence H description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 45) chain D residue 1519 type sequence D description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 46) chain D residue 1558 type sequence L description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 47) chain D residue 1561 type sequence F description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 48) chain D residue 1565 type sequence F description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 49) chain D residue 1602 type sequence Y description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 50) chain D residue 1603 type sequence S description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 51) chain D residue 1606 type sequence L description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 52) chain D residue 1655 type sequence M description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 53) chain D residue 1683 type sequence A description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 54) chain D residue 1684 type sequence G description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 55) chain D residue 1714 type sequence H description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 56) chain D residue 1717 type sequence E description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 57) chain D residue 1738 type sequence H description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 58) chain D residue 1795 type sequence D description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 59) chain D residue 1796 type sequence D description BINDING SITE FOR RESIDUE DCF D 1853 source : AC8 60) chain B residue 515 type catalytic sequence H description 376 source MCSA : MCSA2 61) chain B residue 517 type catalytic sequence H description 376 source MCSA : MCSA2 62) chain B residue 714 type catalytic sequence H description 376 source MCSA : MCSA2 63) chain B residue 717 type catalytic sequence E description 376 source MCSA : MCSA2 64) chain B residue 738 type catalytic sequence H description 376 source MCSA : MCSA2 65) chain B residue 795 type catalytic sequence D description 376 source MCSA : MCSA2 66) chain D residue 1515 type catalytic sequence H description 376 source MCSA : MCSA4 67) chain D residue 1517 type catalytic sequence H description 376 source MCSA : MCSA4 68) chain D residue 1714 type catalytic sequence H description 376 source MCSA : MCSA4 69) chain D residue 1717 type catalytic sequence E description 376 source MCSA : MCSA4 70) chain D residue 1738 type catalytic sequence H description 376 source MCSA : MCSA4 71) chain D residue 1795 type catalytic sequence D description 376 source MCSA : MCSA4 72) 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 73) 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 74) 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 75) 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 76) chain B residue 515 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 77) chain B residue 517 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 78) chain B residue 714 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 79) chain B residue 795 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 80) chain B residue 519 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 81) 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 82) chain B residue 684 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 83) 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 84) chain B residue 554 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00813 source Swiss-Prot : SWS_FT_FI8 85) chain B residue 732 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00813 source Swiss-Prot : SWS_FT_FI8 86) chain D residue 1554 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00813 source Swiss-Prot : SWS_FT_FI8 87) chain D residue 1732 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00813 source Swiss-Prot : SWS_FT_FI8 88) chain B residue 796 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 89) 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 90) chain B residue 717 type ACT_SITE sequence E description Proton donor => ECO:0000305|PubMed:8634299, ECO:0000305|PubMed:9622483 source Swiss-Prot : SWS_FT_FI1 91) 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 92) chain B residue 558 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 93) chain B residue 562 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 94) 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 95) 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 96) chain B residue 738 type SITE sequence H description Important for catalytic activity => ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483 source Swiss-Prot : SWS_FT_FI7 97) 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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