eF-site ID 1sft-AB PDB Code 1sft Chain A, B click to enlarge Title ALANINE RACEMASE Classification ISOMERASE Compound ALANINE RACEMASE Source Geobacillus stearothermophilus (Bacillus stearothermophilus) (ALR_BACST) Sequence A:  NDFHRDTWAEVDLDAIYDNVENLRRLLPDDTHIMAVVKAN AYGHGDVQVARTALEAGASRLAVAFLDEALALREKGIEAP ILVLGASRPADAALAAQQRIALTVFRSDWLEEASALYSGP FPIHFHLKMDTGMGRLGVKDEEETKRIVALIERHPHFVLE GLYTHFATADEVNTDYFSYQYTRFLHMLEWLPSRPPLVHC ANSAASLRFPDRTFNMVRFGIAMYGLAPSPGIKPLLPYPL KEAFSLHSRLVHVKKLQPGEKVSYGATYTAQTEEWIGTIP IGYADGWLRRLQHFHVLVDGQKAPIVGRICMDQCMIRLPG PLPVGTKVTLIGRQGDEVISIDDVARHLETINYEVPCTIS YRVPRIFFRHKRIMEVRNAIGA B:  NDFHRDTWAEVDLDAIYDNVENLRRLLPDDTHIMAVVKAN AYGHGDVQVARTALEAGASRLAVAFLDEALALREKGIEAP ILVLGASRPADAALAAQQRIALTVFRSDWLEEASALYSGP FPIHFHLKMDTGMGRLGVKDEEETKRIVALIERHPHFVLE GLYTHFATADEVNTDYFSYQYTRFLHMLEWLPSRPPLVHC ANSAASLRFPDRTFNMVRFGIAMYGLAPSPGIKPLLPYPL KEAFSLHSRLVHVKKLQPGEKVSYGATYTAQTEEWIGTIP IGYADGWLRRLQHFHVLVDGQKAPIVGRICMDQCMIRLPG PLPVGTKVTLIGRQGDEVISIDDVARHLETINYEVPCTIS YRVPRIFFRHKRIMEVRNAI Description (1)  ALANINE RACEMASE, PYRIDOXAL-5'-PHOSPHATE Functional site 1) chain A residue 39 type sequence K description BINDING SITE FOR RESIDUE ACT B 400 source : AC1 2) chain A residue 136 type sequence R description BINDING SITE FOR RESIDUE ACT B 400 source : AC1 3) chain B residue 265 type sequence Y description BINDING SITE FOR RESIDUE ACT B 400 source : AC1 4) chain B residue 311 type sequence C description BINDING SITE FOR RESIDUE ACT B 400 source : AC1 5) chain B residue 312 type sequence M description BINDING SITE FOR RESIDUE ACT B 400 source : AC1 6) chain A residue 265 type sequence Y description BINDING SITE FOR RESIDUE ACT A 401 source : AC2 7) chain A residue 284 type sequence Y description BINDING SITE FOR RESIDUE ACT A 401 source : AC2 8) chain A residue 311 type sequence C description BINDING SITE FOR RESIDUE ACT A 401 source : AC2 9) chain A residue 312 type sequence M description BINDING SITE FOR RESIDUE ACT A 401 source : AC2 10) chain B residue 39 type sequence K description BINDING SITE FOR RESIDUE ACT A 401 source : AC2 11) chain B residue 136 type sequence R description BINDING SITE FOR RESIDUE ACT A 401 source : AC2 12) chain A residue 39 type sequence K description BINDING SITE FOR RESIDUE PLP A 402 source : AC3 13) chain A residue 43 type sequence Y description BINDING SITE FOR RESIDUE PLP A 402 source : AC3 14) chain A residue 85 type sequence L description BINDING SITE FOR RESIDUE PLP A 402 source : AC3 15) chain A residue 136 type sequence R description BINDING SITE FOR RESIDUE PLP A 402 source : AC3 16) chain A residue 166 type sequence H description BINDING SITE FOR RESIDUE PLP A 402 source : AC3 17) chain A residue 204 type sequence S description BINDING SITE FOR RESIDUE PLP A 402 source : AC3 18) chain A residue 219 type sequence R description BINDING SITE FOR RESIDUE PLP A 402 source : AC3 19) chain A residue 221 type sequence G description BINDING SITE FOR RESIDUE PLP A 402 source : AC3 20) chain A residue 222 type sequence I description BINDING SITE FOR RESIDUE PLP A 402 source : AC3 21) chain A residue 354 type sequence Y description BINDING SITE FOR RESIDUE PLP A 402 source : AC3 22) chain B residue 39 type sequence K description BINDING SITE FOR RESIDUE PLP B 401 source : AC4 23) chain B residue 43 type sequence Y description BINDING SITE FOR RESIDUE PLP B 401 source : AC4 24) chain B residue 85 type sequence L description BINDING SITE FOR RESIDUE PLP B 401 source : AC4 25) chain B residue 136 type sequence R description BINDING SITE FOR RESIDUE PLP B 401 source : AC4 26) chain B residue 166 type sequence H description BINDING SITE FOR RESIDUE PLP B 401 source : AC4 27) chain B residue 203 type sequence N description BINDING SITE FOR RESIDUE PLP B 401 source : AC4 28) chain B residue 204 type sequence S description BINDING SITE FOR RESIDUE PLP B 401 source : AC4 29) chain B residue 219 type sequence R description BINDING SITE FOR RESIDUE PLP B 401 source : AC4 30) chain B residue 221 type sequence G description BINDING SITE FOR RESIDUE PLP B 401 source : AC4 31) chain B residue 222 type sequence I description BINDING SITE FOR RESIDUE PLP B 401 source : AC4 32) chain B residue 354 type sequence Y description BINDING SITE FOR RESIDUE PLP B 401 source : AC4 33) chain A residue 39 type catalytic sequence K description 213 source MCSA : MCSA1 34) chain A residue 136 type catalytic sequence R description 213 source MCSA : MCSA1 35) chain A residue 166 type catalytic sequence H description 213 source MCSA : MCSA1 36) chain A residue 219 type catalytic sequence R description 213 source MCSA : MCSA1 37) chain A residue 265 type catalytic sequence Y description 213 source MCSA : MCSA1 38) chain A residue 311 type catalytic sequence C description 213 source MCSA : MCSA1 39) chain A residue 313 type catalytic sequence D description 213 source MCSA : MCSA1 40) chain B residue 39 type catalytic sequence K description 213 source MCSA : MCSA2 41) chain B residue 136 type catalytic sequence R description 213 source MCSA : MCSA2 42) chain B residue 166 type catalytic sequence H description 213 source MCSA : MCSA2 43) chain B residue 219 type catalytic sequence R description 213 source MCSA : MCSA2 44) chain B residue 265 type catalytic sequence Y description 213 source MCSA : MCSA2 45) chain B residue 311 type catalytic sequence C description 213 source MCSA : MCSA2 46) chain B residue 313 type catalytic sequence D description 213 source MCSA : MCSA2 47) chain A residue 39 type ACT_SITE sequence K description Proton acceptor; specific for D-alanine => ECO:0000305|PubMed:10502689, ECO:0000305|PubMed:15807525 source Swiss-Prot : SWS_FT_FI1 48) chain B residue 39 type ACT_SITE sequence K description Proton acceptor; specific for D-alanine => ECO:0000305|PubMed:10502689, ECO:0000305|PubMed:15807525 source Swiss-Prot : SWS_FT_FI1 49) chain A residue 265 type ACT_SITE sequence Y description Proton acceptor; specific for L-alanine => ECO:0000305|PubMed:10502689, ECO:0000305|PubMed:15807525 source Swiss-Prot : SWS_FT_FI2 50) chain B residue 265 type ACT_SITE sequence Y description Proton acceptor; specific for L-alanine => ECO:0000305|PubMed:10502689, ECO:0000305|PubMed:15807525 source Swiss-Prot : SWS_FT_FI2 51) chain A residue 136 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11886871 source Swiss-Prot : SWS_FT_FI3 52) chain A residue 312 type BINDING sequence M description BINDING => ECO:0000269|PubMed:11886871 source Swiss-Prot : SWS_FT_FI3 53) chain B residue 136 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11886871 source Swiss-Prot : SWS_FT_FI3 54) chain B residue 312 type BINDING sequence M description BINDING => ECO:0000269|PubMed:11886871 source Swiss-Prot : SWS_FT_FI3 55) chain A residue 39 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11886871, ECO:0000269|PubMed:15807525, ECO:0000269|PubMed:9063881 source Swiss-Prot : SWS_FT_FI4 56) chain B residue 39 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11886871, ECO:0000269|PubMed:15807525, ECO:0000269|PubMed:9063881 source Swiss-Prot : SWS_FT_FI4 57) chain A residue 129 type MOD_RES sequence K description N6-carboxylysine => ECO:0000269|PubMed:10079072, ECO:0000269|PubMed:11886871, ECO:0000269|PubMed:12741835, ECO:0000269|PubMed:15807525, ECO:0000269|Ref.10 source Swiss-Prot : SWS_FT_FI5 58) chain B residue 129 type MOD_RES sequence K description N6-carboxylysine => ECO:0000269|PubMed:10079072, ECO:0000269|PubMed:11886871, ECO:0000269|PubMed:12741835, ECO:0000269|PubMed:15807525, ECO:0000269|Ref.10 source Swiss-Prot : SWS_FT_FI5 59) chain A residue 36-46 type prosite sequence AVVKANAYGHG description ALANINE_RACEMASE Alanine racemase pyridoxal-phosphate attachment site. AVvKANAYGHG source prosite : PS00395

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