eF-site ID 1a4l-B PDB Code 1a4l Chain B 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 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 B residue 515 type sequence H description BINDING SITE FOR RESIDUE ZN B 900 source : AC3 11) chain B residue 517 type sequence H description BINDING SITE FOR RESIDUE ZN B 900 source : AC3 12) chain B residue 714 type sequence H description BINDING SITE FOR RESIDUE ZN B 900 source : AC3 13) chain B residue 795 type sequence D description BINDING SITE FOR RESIDUE ZN B 900 source : AC3 14) chain B residue 517 type sequence H description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 15) chain B residue 519 type sequence D description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 16) chain B residue 558 type sequence L description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 17) chain B residue 561 type sequence F description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 18) chain B residue 562 type sequence L description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 19) chain B residue 565 type sequence F description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 20) chain B residue 602 type sequence Y description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 21) chain B residue 603 type sequence S description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 22) chain B residue 606 type sequence L description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 23) chain B residue 655 type sequence M description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 24) chain B residue 683 type sequence A description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 25) chain B residue 684 type sequence G description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 26) chain B residue 714 type sequence H description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 27) chain B residue 717 type sequence E description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 28) chain B residue 738 type sequence H description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 29) chain B residue 795 type sequence D description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 30) chain B residue 796 type sequence D description BINDING SITE FOR RESIDUE DCF B 853 source : AC6 31) chain B residue 515 type catalytic sequence H description 376 source MCSA : MCSA2 32) chain B residue 517 type catalytic sequence H description 376 source MCSA : MCSA2 33) chain B residue 714 type catalytic sequence H description 376 source MCSA : MCSA2 34) chain B residue 717 type catalytic sequence E description 376 source MCSA : MCSA2 35) chain B residue 738 type catalytic sequence H description 376 source MCSA : MCSA2 36) chain B residue 795 type catalytic sequence D description 376 source MCSA : MCSA2 37) 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 38) 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 39) 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 40) 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 41) 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 42) 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 43) chain B residue 554 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00813 source Swiss-Prot : SWS_FT_FI8 44) chain B residue 732 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00813 source Swiss-Prot : SWS_FT_FI8 45) 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 46) 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 47) 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 48) 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 49) 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

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