eF-site ID 1a0g-B PDB Code 1a0g Chain B click to enlarge Title L201A MUTANT OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAMINE-5'-PHOSPHATE Classification TRANSFERASE Compound D-AMINO ACID AMINOTRANSFERASE Source Bacillus sp. (strain YM-1) (DAAA_BACYM) Sequence B:  GYTLWNDQIVKDEEVKIDKEDRGYQFGDGVYEVVKVYNGE MFTVNEHIDRLYASAEKIRITIPYTKDKFHQLLHELVEKN ELNTGHIYFQVTRGTSPRAHQFPENTVKPVIIGYTKENPR PLENLEKGVKATFVEDIRWLRCDIKSLNLLGAVLAKQEAH EKGCYEAILHRNNTVTEGSSSNVFGIKDGILYTHPANNMI AKGITRDVVIACANEINMPVKEIPFTTHEALKMDELFVTS TTSEITPVIEIDGKLIRDGKVGEWTRKLQKQFETKIPKPL HI Description Functional site 1) chain B residue 98 type sequence R description AN ACTIVE SITE FOR SUBUNIT A. source : ASA 2) chain B residue 145 type sequence K description AN ACTIVE SITE FOR SUBUNIT B. source : ASB 3) chain B residue 31 type sequence Y description AN ACTIVE SITE FOR SUBUNIT B. source : ASB 4) chain B residue 177 type sequence E description AN ACTIVE SITE FOR SUBUNIT B. source : ASB 5) chain B residue 31 type sequence Y description BINDING SITE FOR RESIDUE PMP B 285 source : AC2 6) chain B residue 50 type sequence R description BINDING SITE FOR RESIDUE PMP B 285 source : AC2 7) chain B residue 145 type sequence K description BINDING SITE FOR RESIDUE PMP B 285 source : AC2 8) chain B residue 177 type sequence E description BINDING SITE FOR RESIDUE PMP B 285 source : AC2 9) chain B residue 180 type sequence S description BINDING SITE FOR RESIDUE PMP B 285 source : AC2 10) chain B residue 181 type sequence S description BINDING SITE FOR RESIDUE PMP B 285 source : AC2 11) chain B residue 182 type sequence N description BINDING SITE FOR RESIDUE PMP B 285 source : AC2 12) chain B residue 203 type sequence G description BINDING SITE FOR RESIDUE PMP B 285 source : AC2 13) chain B residue 204 type sequence I description BINDING SITE FOR RESIDUE PMP B 285 source : AC2 14) chain B residue 205 type sequence T description BINDING SITE FOR RESIDUE PMP B 285 source : AC2 15) chain B residue 240 type sequence S description BINDING SITE FOR RESIDUE PMP B 285 source : AC2 16) chain B residue 241 type sequence T description BINDING SITE FOR RESIDUE PMP B 285 source : AC2 17) chain B residue 178 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9538014 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 32 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9538014 source Swiss-Prot : SWS_FT_FI2 19) chain B residue 51 type BINDING sequence L description BINDING => ECO:0000269|PubMed:9538014 source Swiss-Prot : SWS_FT_FI2 20) chain B residue 99 type BINDING sequence A description BINDING => ECO:0000269|PubMed:9538014 source Swiss-Prot : SWS_FT_FI2 21) chain B residue 101 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:9538014 source Swiss-Prot : SWS_FT_FI2 22) chain B residue 146 type ACT_SITE sequence S description Proton acceptor => ECO:0000269|PubMed:7626635 source Swiss-Prot : SWS_FT_FI1 23) chain B residue 146 type MOD_RES sequence S description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:7626635 source Swiss-Prot : SWS_FT_FI3 24) chain B residue 32 type catalytic sequence E description 66 source MCSA : MCSA2 25) chain B residue 146 type catalytic sequence S description 66 source MCSA : MCSA2 26) chain B residue 178 type catalytic sequence G description 66 source MCSA : MCSA2 27) chain B residue 202 type catalytic sequence K description 66 source MCSA : MCSA2

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