eF-site ID 1fkx-A PDB Code 1fkx Chain A click to enlarge Title MURINE ADENOSINE DEAMINASE (D296A) Classification AMINOHYDROLASE Compound ADENOSINE DEAMINASE Source Mus musculus (Mouse) (ADA_MOUSE) Sequence A:  TPAFNKPKVELHVHLDGAIKPETILYFGKKRGIALPADTV EELRNIIGMDKPLSLPGFLAKFDYYMPVIAGCREAIKRIA YEFVEMKAKEGVVYVEVRYSPHLLANSKVDPMPWNQTEGD VTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRHQPSWSL EVLELCKKYNQKTVVAMDLAGDETIEGSSLFPGHVEAYEG AVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTI EDEALYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRF KNDKANYSLNTDAPLIFKSTLDTDYQMTKKDMGFTEEEFK RLNINAAKSSFLPEEEKKELLERLYREYQ 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 PRH A 353 source : AC2 6) chain A residue 19 type sequence D description BINDING SITE FOR RESIDUE PRH A 353 source : AC2 7) chain A residue 61 type sequence F description BINDING SITE FOR RESIDUE PRH A 353 source : AC2 8) chain A residue 65 type sequence F description BINDING SITE FOR RESIDUE PRH A 353 source : AC2 9) chain A residue 106 type sequence L description BINDING SITE FOR RESIDUE PRH A 353 source : AC2 10) chain A residue 155 type sequence M description BINDING SITE FOR RESIDUE PRH A 353 source : AC2 11) chain A residue 184 type sequence G description BINDING SITE FOR RESIDUE PRH A 353 source : AC2 12) chain A residue 214 type sequence H description BINDING SITE FOR RESIDUE PRH A 353 source : AC2 13) chain A residue 217 type sequence E description BINDING SITE FOR RESIDUE PRH A 353 source : AC2 14) chain A residue 238 type sequence H description BINDING SITE FOR RESIDUE PRH A 353 source : AC2 15) chain A residue 295 type sequence D description BINDING SITE FOR RESIDUE PRH A 353 source : AC2 16) chain A residue 15 type catalytic sequence H description 376 source MCSA : MCSA1 17) chain A residue 17 type catalytic sequence H description 376 source MCSA : MCSA1 18) chain A residue 214 type catalytic sequence H description 376 source MCSA : MCSA1 19) chain A residue 217 type catalytic sequence E description 376 source MCSA : MCSA1 20) chain A residue 238 type catalytic sequence H description 376 source MCSA : MCSA1 21) chain A residue 295 type catalytic sequence D description 376 source MCSA : MCSA1 22) 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 23) 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 24) 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 25) 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 26) 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 27) 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 28) 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 29) chain A residue 296 type BINDING sequence A description BINDING => ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1UIP source Swiss-Prot : SWS_FT_FI5 30) chain A residue 54 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00813 source Swiss-Prot : SWS_FT_FI8 31) chain A residue 232 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00813 source Swiss-Prot : SWS_FT_FI8 32) 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 33) 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 34) 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

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