eF-site ID 1b8g-AB PDB Code 1b8g Chain A, B click to enlarge Title 1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE Classification LYASE Compound PROTEIN (1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE) Source (1A1C_MALDO) Sequence A:  MLSRNATSSYFLGWQEYEKNPYHEVHNTNGIIQMGLAENQ LCFDLLESWLAKNPEAAAFKKNGESIFAELALFQDYHGLP AFKKAMVDFMAEIRGNKVTFDPNHLVLTAGATSANETFIF CLADPGEAVLIPTPYYPGFDRDLKWRTGVEIVPIHCTSSN GFQITETALEEAYQEAEKRNLRVKGVLVTNPSNPLGTTMT RNELYLLLSFVEDKGIHLISDEIYSGTAFSSPSFISVMEV LKDRNCDENSEVWQRVHVVYSLSKDLGLPGFRVGAIYSND DMVVAAATKMSSFGLVSSQTQHLLSAMLSDKKLTKNYIAE NHKRLKQRQKKLVSGLQKSGISCLNGNAGLFCWVDMRHLL RSNTFEAEMELWKKIVYEVHLNISPGSSCHCTEPGWFRVC FANLPERTLDLAMQRLKAFVG B:  MLSRNATFNSSSYFLGWQEYEKNPYHEVHNTNGIIQMGLA ENQLCFDLLESWLAKNPEAAAFKKNGESIFAELALFQDYH GLPAFKKAMVDFMAEIRGNKVTFDPNHLVLTAGATSANET FIFCLADPGEAVLIPTPYYPGFDRDLKWRTGVEIVPIHCT SSNGFQITETALEEAYQEAEKRNLRVKGVLVTNPSNPLGT TMTRNELYLLLSFVEDKGIHLISDEIYSGTAFSSPSFISV MEVLKDRNCDENSEVWQRVHVVYSLSKDLGLPGFRVGAIY SNDDMVVAAATKMSSFGLVSSQTQHLLSAMLSDKKLTKNY IAENHKRLKQRQKKLVSGLQKSGISCLNGNAGLFCWVDMR HLLRSNTFEAEMELWKKIVYEVHLNISPGSSCHCTEPGWF RVCFANLPERTLDLAMQRLKAFVGE Description Functional site 1) chain B residue 85 type sequence Y description IN THE ACTIVE SITE OF ONE SUBUNIT, TYR 85 IS CONTRIBUTED BY THE OPPOSITE SUBUNIT source : ACT 2) chain A residue 121 type sequence T description IN THE ACTIVE SITE OF ONE SUBUNIT, TYR 85 IS CONTRIBUTED BY THE OPPOSITE SUBUNIT source : ACT 3) chain A residue 202 type sequence N description IN THE ACTIVE SITE OF ONE SUBUNIT, TYR 85 IS CONTRIBUTED BY THE OPPOSITE SUBUNIT source : ACT 4) chain A residue 230 type sequence D description IN THE ACTIVE SITE OF ONE SUBUNIT, TYR 85 IS CONTRIBUTED BY THE OPPOSITE SUBUNIT source : ACT 5) chain A residue 233 type sequence Y description IN THE ACTIVE SITE OF ONE SUBUNIT, TYR 85 IS CONTRIBUTED BY THE OPPOSITE SUBUNIT source : ACT 6) chain A residue 270 type sequence S description IN THE ACTIVE SITE OF ONE SUBUNIT, TYR 85 IS CONTRIBUTED BY THE OPPOSITE SUBUNIT source : ACT 7) chain A residue 273 type sequence K description IN THE ACTIVE SITE OF ONE SUBUNIT, TYR 85 IS CONTRIBUTED BY THE OPPOSITE SUBUNIT source : ACT 8) chain A residue 281 type sequence R description IN THE ACTIVE SITE OF ONE SUBUNIT, TYR 85 IS CONTRIBUTED BY THE OPPOSITE SUBUNIT source : ACT 9) chain A residue 407 type sequence R description IN THE ACTIVE SITE OF ONE SUBUNIT, TYR 85 IS CONTRIBUTED BY THE OPPOSITE SUBUNIT source : ACT 10) chain A residue 119 type sequence G description BINDING SITE FOR RESIDUE PLP A 500 source : AC1 11) chain A residue 120 type sequence A description BINDING SITE FOR RESIDUE PLP A 500 source : AC1 12) chain A residue 121 type sequence T description BINDING SITE FOR RESIDUE PLP A 500 source : AC1 13) chain A residue 145 type sequence Y description BINDING SITE FOR RESIDUE PLP A 500 source : AC1 14) chain A residue 202 type sequence N description BINDING SITE FOR RESIDUE PLP A 500 source : AC1 15) chain A residue 230 type sequence D description BINDING SITE FOR RESIDUE PLP A 500 source : AC1 16) chain A residue 232 type sequence I description BINDING SITE FOR RESIDUE PLP A 500 source : AC1 17) chain A residue 233 type sequence Y description BINDING SITE FOR RESIDUE PLP A 500 source : AC1 18) chain A residue 270 type sequence S description BINDING SITE FOR RESIDUE PLP A 500 source : AC1 19) chain A residue 272 type sequence S description BINDING SITE FOR RESIDUE PLP A 500 source : AC1 20) chain A residue 273 type sequence K description BINDING SITE FOR RESIDUE PLP A 500 source : AC1 21) chain A residue 281 type sequence R description BINDING SITE FOR RESIDUE PLP A 500 source : AC1 22) chain B residue 119 type sequence G description BINDING SITE FOR RESIDUE PLP B 500 source : AC2 23) chain B residue 120 type sequence A description BINDING SITE FOR RESIDUE PLP B 500 source : AC2 24) chain B residue 121 type sequence T description BINDING SITE FOR RESIDUE PLP B 500 source : AC2 25) chain B residue 145 type sequence Y description BINDING SITE FOR RESIDUE PLP B 500 source : AC2 26) chain B residue 202 type sequence N description BINDING SITE FOR RESIDUE PLP B 500 source : AC2 27) chain B residue 232 type sequence I description BINDING SITE FOR RESIDUE PLP B 500 source : AC2 28) chain B residue 233 type sequence Y description BINDING SITE FOR RESIDUE PLP B 500 source : AC2 29) chain B residue 270 type sequence S description BINDING SITE FOR RESIDUE PLP B 500 source : AC2 30) chain B residue 272 type sequence S description BINDING SITE FOR RESIDUE PLP B 500 source : AC2 31) chain B residue 273 type sequence K description BINDING SITE FOR RESIDUE PLP B 500 source : AC2 32) chain B residue 281 type sequence R description BINDING SITE FOR RESIDUE PLP B 500 source : AC2 33) chain A residue 145 type catalytic sequence Y description 418 source MCSA : MCSA1 34) chain A residue 230 type catalytic sequence D description 418 source MCSA : MCSA1 35) chain A residue 232 type catalytic sequence I description 418 source MCSA : MCSA1 36) chain A residue 273 type catalytic sequence K description 418 source MCSA : MCSA1 37) chain B residue 145 type catalytic sequence Y description 418 source MCSA : MCSA2 38) chain B residue 230 type catalytic sequence D description 418 source MCSA : MCSA2 39) chain B residue 232 type catalytic sequence I description 418 source MCSA : MCSA2 40) chain B residue 273 type catalytic sequence K description 418 source MCSA : MCSA2 41) chain A residue 84 type BINDING sequence D description BINDING => ECO:0000305|PubMed:12686108, ECO:0007744|PDB:1M4N source Swiss-Prot : SWS_FT_FI1 42) chain B residue 84 type BINDING sequence D description BINDING => ECO:0000305|PubMed:12686108, ECO:0007744|PDB:1M4N source Swiss-Prot : SWS_FT_FI1 43) chain A residue 145 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:12686108, ECO:0007744|PDB:1B8G, ECO:0007744|PDB:1M4N source Swiss-Prot : SWS_FT_FI2 44) chain A residue 151 type BINDING sequence D description BINDING => ECO:0000305|PubMed:12686108, ECO:0007744|PDB:1B8G, ECO:0007744|PDB:1M4N source Swiss-Prot : SWS_FT_FI2 45) chain B residue 145 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:12686108, ECO:0007744|PDB:1B8G, ECO:0007744|PDB:1M4N source Swiss-Prot : SWS_FT_FI2 46) chain B residue 151 type BINDING sequence D description BINDING => ECO:0000305|PubMed:12686108, ECO:0007744|PDB:1B8G, ECO:0007744|PDB:1M4N source Swiss-Prot : SWS_FT_FI2 47) chain A residue 270-283 type prosite sequence SLSKDLGLPGFRVG description AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SLSKdlGLpGFRVG source prosite : PS00105 48) chain A residue 273 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10610793, ECO:0000269|PubMed:9398277, ECO:0007744|PDB:1B8G, ECO:0007744|PDB:3PIU source Swiss-Prot : SWS_FT_FI3 49) chain B residue 273 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10610793, ECO:0000269|PubMed:9398277, ECO:0007744|PDB:1B8G, ECO:0007744|PDB:3PIU source Swiss-Prot : SWS_FT_FI3

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