eF-site ID 1g2w-B PDB Code 1g2w Chain 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 B:  GYTLWNDQIVKDEEVKIDKEDRGYQFGDGVYEVVKVYNGE MFTVNEHIDRLYASAEKIRITIPYTKDKFHQLLHELVEKN ELNTGHIYFQVTRGTSPRAHQFPENTVKPVIIGYTKENPR PLENLEKGVKATFVEDIRWLRCDIKSLNLLGAVLAKQEAH EKGCYEAILHRNNTVTSGSSSNVFGIKDGILYTHPANNMI LKGITRDVVIACANEINMPVKEIPFTTHEALKMDELFVTS TTSEITPVIEIDGKLIRDGKVGEWTRKLQKQFETKIP Description Functional site 1) chain B residue 31 type sequence Y description BINDING SITE FOR RESIDUE ACT A 900 source : AC1 2) chain B residue 98 type sequence R description BINDING SITE FOR RESIDUE ACT A 901 source : AC2 3) chain B residue 100 type sequence H description BINDING SITE FOR RESIDUE ACT A 901 source : AC2 4) chain B residue 31 type sequence Y description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 5) chain B residue 47 type sequence H description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 6) chain B residue 50 type sequence R description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 7) chain B residue 138 type sequence R description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 8) chain B residue 180 type sequence S description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 9) chain B residue 181 type sequence S description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 10) chain B residue 203 type sequence G description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 11) chain B residue 204 type sequence I description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 12) chain B residue 205 type sequence T description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 13) chain B residue 240 type sequence S description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 14) chain B residue 241 type sequence T description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 15) chain B residue 445 type sequence K description BINDING SITE FOR RESIDUE PLP B 585 source : AC4 16) chain B residue 32 type catalytic sequence E description 66 source MCSA : MCSA2 17) chain B residue 146 type catalytic sequence S description 66 source MCSA : MCSA2 18) chain B residue 178 type catalytic sequence G description 66 source MCSA : MCSA2 19) chain B residue 202 type catalytic sequence K description 66 source MCSA : MCSA2 20) chain B residue 146 type ACT_SITE sequence S description Proton acceptor => ECO:0000269|PubMed:7626635 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 32 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9538014 source Swiss-Prot : SWS_FT_FI2 22) chain B residue 178 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9538014 source Swiss-Prot : SWS_FT_FI2 23) chain B residue 51 type BINDING sequence L description BINDING => ECO:0000269|PubMed:9538014 source Swiss-Prot : SWS_FT_FI2 24) chain B residue 99 type BINDING sequence A description BINDING => ECO:0000269|PubMed:9538014 source Swiss-Prot : SWS_FT_FI2 25) chain B residue 101 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:9538014 source Swiss-Prot : SWS_FT_FI2 26) 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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