eF-site ID 1g2w-AB PDB Code 1g2w Chain A, B click to enlarge Title E177S MUTANT OF THE PYRIDOXAL-5'-PHOSPHATE ENZYME D-AMINO ACID AMINOTRANSFERASE Classification TRANSFERASE Compound D-ALANINE AMINOTRANSFERASE Source (P83771_BACST) Sequence A:  GYTLWNDQIVKDEEVKIDKEDRGYQFGDGVYEVVKVYNGE MFTVNEHIDRLYASAEKIRITIPYTKDKFHQLLHELVEKN ELNTGHIYFQVTRGTSPRAHQFPENTVKPVIIGYTKENPR PLENLEKGVKATFVEDIRWLRCDIKSLNLLGAVLAKQEAH EKGCYEAILHRNNTVTSGSSSNVFGIKDGILYTHPANNMI LKGITRDVVIACANEINMPVKEIPFTTHEALKMDELFVTS TTSEITPVIEIDGKLIRDGKVGEWTRKLQKQFETKIP B:  GYTLWNDQIVKDEEVKIDKEDRGYQFGDGVYEVVKVYNGE MFTVNEHIDRLYASAEKIRITIPYTKDKFHQLLHELVEKN ELNTGHIYFQVTRGTSPRAHQFPENTVKPVIIGYTKENPR PLENLEKGVKATFVEDIRWLRCDIKSLNLLGAVLAKQEAH EKGCYEAILHRNNTVTSGSSSNVFGIKDGILYTHPANNMI LKGITRDVVIACANEINMPVKEIPFTTHEALKMDELFVTS TTSEITPVIEIDGKLIRDGKVGEWTRKLQKQFETKIP Description Functional site 1) chain A residue 98 type sequence R description BINDING SITE FOR RESIDUE ACT A 900 source : AC1 2) chain A residue 100 type sequence H description BINDING SITE FOR RESIDUE ACT A 900 source : AC1 3) chain B residue 31 type sequence Y description BINDING SITE FOR RESIDUE ACT A 900 source : AC1 4) chain A residue 31 type sequence Y description BINDING SITE FOR RESIDUE ACT A 901 source : AC2 5) chain B residue 98 type sequence R description BINDING SITE FOR RESIDUE ACT A 901 source : AC2 6) chain B residue 100 type sequence H description BINDING SITE FOR RESIDUE ACT A 901 source : AC2 7) chain A residue 31 type sequence Y description BINDING SITE FOR RESIDUE PLP A 285 source : AC3 8) chain A residue 47 type sequence H description BINDING SITE FOR RESIDUE PLP A 285 source : AC3 9) chain A residue 50 type sequence R description BINDING SITE FOR RESIDUE PLP A 285 source : AC3 10) chain A residue 138 type sequence R description BINDING SITE FOR RESIDUE PLP A 285 source : AC3 11) chain A residue 145 type sequence K description BINDING SITE FOR RESIDUE PLP A 285 source : AC3 12) chain A residue 179 type sequence S description BINDING SITE FOR RESIDUE PLP A 285 source : AC3 13) chain A residue 180 type sequence S description BINDING SITE FOR RESIDUE PLP A 285 source : AC3 14) chain A residue 181 type sequence S description BINDING SITE FOR RESIDUE PLP A 285 source : AC3 15) chain A residue 201 type sequence L description BINDING SITE FOR RESIDUE PLP A 285 source : AC3 16) chain A residue 203 type sequence G description BINDING SITE FOR RESIDUE PLP A 285 source : AC3 17) chain A residue 204 type sequence I description BINDING SITE FOR RESIDUE PLP A 285 source : AC3 18) chain A residue 205 type sequence T description BINDING SITE FOR RESIDUE PLP A 285 source : AC3 19) chain A residue 240 type sequence S description BINDING SITE FOR RESIDUE PLP A 285 source : AC3 20) chain A residue 241 type sequence T description BINDING SITE FOR RESIDUE PLP A 285 source : AC3 21) chain B residue 31 type sequence Y description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 22) chain B residue 47 type sequence H description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 23) chain B residue 50 type sequence R description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 24) chain B residue 138 type sequence R description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 25) chain B residue 180 type sequence S description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 26) chain B residue 181 type sequence S description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 27) chain B residue 203 type sequence G description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 28) chain B residue 204 type sequence I description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 29) chain B residue 205 type sequence T description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 30) chain B residue 240 type sequence S description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 31) chain B residue 241 type sequence T description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 32) chain B residue 445 type sequence K description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 33) chain A residue 32 type catalytic sequence E description 66 source MCSA : MCSA1 34) chain A residue 146 type catalytic sequence S description 66 source MCSA : MCSA1 35) chain A residue 178 type catalytic sequence G description 66 source MCSA : MCSA1 36) chain A residue 202 type catalytic sequence K description 66 source MCSA : MCSA1 37) chain B residue 32 type catalytic sequence E description 66 source MCSA : MCSA2 38) chain B residue 146 type catalytic sequence S description 66 source MCSA : MCSA2 39) chain B residue 178 type catalytic sequence G description 66 source MCSA : MCSA2 40) chain B residue 202 type catalytic sequence K description 66 source MCSA : MCSA2 41) chain A residue 146 type ACT_SITE sequence S description Proton acceptor => ECO:0000269|PubMed:7626635 source Swiss-Prot : SWS_FT_FI1 42) chain B residue 146 type ACT_SITE sequence S description Proton acceptor => ECO:0000269|PubMed:7626635 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 32 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9538014 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 51 type BINDING sequence L description BINDING => ECO:0000269|PubMed:9538014 source Swiss-Prot : SWS_FT_FI2 45) chain A residue 99 type BINDING sequence A description BINDING => ECO:0000269|PubMed:9538014 source Swiss-Prot : SWS_FT_FI2 46) chain A residue 101 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:9538014 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 178 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9538014 source Swiss-Prot : SWS_FT_FI2 48) chain B residue 32 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9538014 source Swiss-Prot : SWS_FT_FI2 49) chain B residue 178 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9538014 source Swiss-Prot : SWS_FT_FI2 50) chain B residue 51 type BINDING sequence L description BINDING => ECO:0000269|PubMed:9538014 source Swiss-Prot : SWS_FT_FI2 51) chain B residue 99 type BINDING sequence A description BINDING => ECO:0000269|PubMed:9538014 source Swiss-Prot : SWS_FT_FI2 52) chain B residue 101 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:9538014 source Swiss-Prot : SWS_FT_FI2 53) chain A residue 146 type MOD_RES sequence S description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:7626635 source Swiss-Prot : SWS_FT_FI3 54) chain B residue 146 type MOD_RES sequence S description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:7626635 source Swiss-Prot : SWS_FT_FI3

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