eF-site ID 3b8w-ABCD PDB Code 3b8w Chain A, B, C, D click to enlarge Title Crystal structure of Escherichia coli alaine racemase mutant E221P Classification ISOMERASE Compound Alanine racemase Source Escherichia coli (strain K12) (ALR1_ECOLI) Sequence A:  MQAATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGH GLLETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEG FFDARDLPTISAQHFHTAVHNEEQLAALEEASLDEPVTVW MXLDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHF ARADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLW PQSHFDWVRPGIILYGVSPLPDRSTGADFGCQPVMSLTSS LIAVREHKAGEPVGYGGTWVSERDTRLGVVAMGYGDGYPR AAPSGTPVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGD PVILWGEGLPVERIAEMTKVSAYELITRLTSRVAMKYVD B:  MQAATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGH GLLETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEG FFDARDLPTISAQHFHTAVHNEEQLAALEEASLDEPVTVW MXLDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHF ARADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLW PQSHFDWVRPGIILYGVSPLPDRSTGADFGCQPVMSLTSS LIAVREHKAGEPVGYGGTWVSERDTRLGVVAMGYGDGYPR AAPSGTPVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGD PVILWGEGLPVERIAEMTKVSAYELITRLTSRVAMKYVD C:  AATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGHGL LETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEGFF DARDLPTISAQHFHTAVHNEEQLAALEEASLDEPVTVWMX LDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHFAR ADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLWPQ SHFDWVRPGIILYGVSPLPDRSTGADFGCQPVMSLTSSLI AVREHKAGEPVGYGGTWVSERDTRLGVVAMGYGDGYPRAA PSGTPVVPIVGRVAMDMICVDLGPQAQDKAGDPVILWGEG LPVERIKVSAYELITRLTSRVAMKYVD D:  AATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGHGL LETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEGFF DARDLPTISAQHFHTAVHNEEQLAALEEASLDEPVTVWMX LDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHFAR ADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLWPQ SHFDWVRPGIILYGVSPLPDRSTGADFGCQPVMSLTSSLI AVREHKAGEPVGYGGTWVSERDTRLGVVAMGYGDGYPRAA PSGTPVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGDPV ILWGEGLPVERIKVSAYELITRLTSRVAMKYVD Description Functional site 1) chain A residue 19 type sequence R description BINDING SITE FOR RESIDUE SO4 A 360 source : AC1 2) chain B residue 266 type sequence R description BINDING SITE FOR RESIDUE SO4 A 360 source : AC1 3) chain A residue 162 type sequence R description BINDING SITE FOR RESIDUE SO4 A 361 source : AC2 4) chain A residue 343 type sequence Y description BINDING SITE FOR RESIDUE SO4 B 360 source : AC3 5) chain B residue 255 type sequence Y description BINDING SITE FOR RESIDUE SO4 B 360 source : AC3 6) chain B residue 274 type sequence Y description BINDING SITE FOR RESIDUE SO4 B 360 source : AC3 7) chain B residue 280 type sequence R description BINDING SITE FOR RESIDUE SO4 B 360 source : AC3 8) chain A residue 266 type sequence R description BINDING SITE FOR RESIDUE SO4 B 361 source : AC4 9) chain B residue 19 type sequence R description BINDING SITE FOR RESIDUE SO4 B 361 source : AC4 10) chain C residue 19 type sequence R description BINDING SITE FOR RESIDUE SO4 C 360 source : AC5 11) chain D residue 266 type sequence R description BINDING SITE FOR RESIDUE SO4 C 360 source : AC5 12) chain C residue 162 type sequence R description BINDING SITE FOR RESIDUE SO4 C 361 source : AC6 13) chain C residue 168 type sequence C description BINDING SITE FOR RESIDUE SO4 C 361 source : AC6 14) chain D residue 162 type sequence R description BINDING SITE FOR RESIDUE SO4 D 360 source : AC7 15) chain D residue 168 type sequence C description BINDING SITE FOR RESIDUE SO4 D 360 source : AC7 16) chain A residue 34 type sequence K description BINDING SITE FOR RESIDUE PLP A 1001 source : AC8 17) chain A residue 38 type sequence Y description BINDING SITE FOR RESIDUE PLP A 1001 source : AC8 18) chain A residue 159 type sequence H description BINDING SITE FOR RESIDUE PLP A 1001 source : AC8 19) chain A residue 193 type sequence A description BINDING SITE FOR RESIDUE PLP A 1001 source : AC8 20) chain A residue 194 type sequence S description BINDING SITE FOR RESIDUE PLP A 1001 source : AC8 21) chain A residue 209 type sequence R description BINDING SITE FOR RESIDUE PLP A 1001 source : AC8 22) chain A residue 211 type sequence G description BINDING SITE FOR RESIDUE PLP A 1001 source : AC8 23) chain A residue 212 type sequence I description BINDING SITE FOR RESIDUE PLP A 1001 source : AC8 24) chain A residue 343 type sequence Y description BINDING SITE FOR RESIDUE PLP A 1001 source : AC8 25) chain B residue 34 type sequence K description BINDING SITE FOR RESIDUE PLP B 1001 source : AC9 26) chain B residue 38 type sequence Y description BINDING SITE FOR RESIDUE PLP B 1001 source : AC9 27) chain B residue 159 type sequence H description BINDING SITE FOR RESIDUE PLP B 1001 source : AC9 28) chain B residue 193 type sequence A description BINDING SITE FOR RESIDUE PLP B 1001 source : AC9 29) chain B residue 194 type sequence S description BINDING SITE FOR RESIDUE PLP B 1001 source : AC9 30) chain B residue 209 type sequence R description BINDING SITE FOR RESIDUE PLP B 1001 source : AC9 31) chain B residue 211 type sequence G description BINDING SITE FOR RESIDUE PLP B 1001 source : AC9 32) chain B residue 212 type sequence I description BINDING SITE FOR RESIDUE PLP B 1001 source : AC9 33) chain B residue 343 type sequence Y description BINDING SITE FOR RESIDUE PLP B 1001 source : AC9 34) chain C residue 34 type sequence K description BINDING SITE FOR RESIDUE PLP C 1001 source : BC1 35) chain C residue 38 type sequence Y description BINDING SITE FOR RESIDUE PLP C 1001 source : BC1 36) chain C residue 78 type sequence L description BINDING SITE FOR RESIDUE PLP C 1001 source : BC1 37) chain C residue 159 type sequence H description BINDING SITE FOR RESIDUE PLP C 1001 source : BC1 38) chain C residue 193 type sequence A description BINDING SITE FOR RESIDUE PLP C 1001 source : BC1 39) chain C residue 194 type sequence S description BINDING SITE FOR RESIDUE PLP C 1001 source : BC1 40) chain C residue 209 type sequence R description BINDING SITE FOR RESIDUE PLP C 1001 source : BC1 41) chain C residue 211 type sequence G description BINDING SITE FOR RESIDUE PLP C 1001 source : BC1 42) chain C residue 212 type sequence I description BINDING SITE FOR RESIDUE PLP C 1001 source : BC1 43) chain C residue 343 type sequence Y description BINDING SITE FOR RESIDUE PLP C 1001 source : BC1 44) chain D residue 34 type sequence K description BINDING SITE FOR RESIDUE PLP D 1001 source : BC2 45) chain D residue 38 type sequence Y description BINDING SITE FOR RESIDUE PLP D 1001 source : BC2 46) chain D residue 159 type sequence H description BINDING SITE FOR RESIDUE PLP D 1001 source : BC2 47) chain D residue 193 type sequence A description BINDING SITE FOR RESIDUE PLP D 1001 source : BC2 48) chain D residue 194 type sequence S description BINDING SITE FOR RESIDUE PLP D 1001 source : BC2 49) chain D residue 209 type sequence R description BINDING SITE FOR RESIDUE PLP D 1001 source : BC2 50) chain D residue 211 type sequence G description BINDING SITE FOR RESIDUE PLP D 1001 source : BC2 51) chain D residue 212 type sequence I description BINDING SITE FOR RESIDUE PLP D 1001 source : BC2 52) chain D residue 343 type sequence Y description BINDING SITE FOR RESIDUE PLP D 1001 source : BC2 53) chain A residue 34 type ACT_SITE sequence K description Proton acceptor; specific for D-alanine => ECO:0000255|HAMAP-Rule:MF_01201 source Swiss-Prot : SWS_FT_FI1 54) chain B residue 34 type ACT_SITE sequence K description Proton acceptor; specific for D-alanine => ECO:0000255|HAMAP-Rule:MF_01201 source Swiss-Prot : SWS_FT_FI1 55) chain C residue 34 type ACT_SITE sequence K description Proton acceptor; specific for D-alanine => ECO:0000255|HAMAP-Rule:MF_01201 source Swiss-Prot : SWS_FT_FI1 56) chain D residue 34 type ACT_SITE sequence K description Proton acceptor; specific for D-alanine => ECO:0000255|HAMAP-Rule:MF_01201 source Swiss-Prot : SWS_FT_FI1 57) chain A residue 255 type ACT_SITE sequence Y description Proton acceptor; specific for L-alanine => ECO:0000255|HAMAP-Rule:MF_01201 source Swiss-Prot : SWS_FT_FI2 58) chain B residue 255 type ACT_SITE sequence Y description Proton acceptor; specific for L-alanine => ECO:0000255|HAMAP-Rule:MF_01201 source Swiss-Prot : SWS_FT_FI2 59) chain C residue 255 type ACT_SITE sequence Y description Proton acceptor; specific for L-alanine => ECO:0000255|HAMAP-Rule:MF_01201 source Swiss-Prot : SWS_FT_FI2 60) chain D residue 255 type ACT_SITE sequence Y description Proton acceptor; specific for L-alanine => ECO:0000255|HAMAP-Rule:MF_01201 source Swiss-Prot : SWS_FT_FI2 61) chain A residue 129 type BINDING sequence R description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 62) chain A residue 303 type BINDING sequence M description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 63) chain B residue 129 type BINDING sequence R description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 64) chain B residue 303 type BINDING sequence M description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 65) chain C residue 129 type BINDING sequence R description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 66) chain C residue 303 type BINDING sequence M description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 67) chain D residue 129 type BINDING sequence R description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 68) chain D residue 303 type BINDING sequence M description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 69) chain A residue 34 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI4 70) chain B residue 34 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI4 71) chain C residue 34 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI4 72) chain D residue 34 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI4 73) chain A residue 122 type MOD_RES sequence X description N6-carboxylysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI5 74) chain B residue 122 type MOD_RES sequence X description N6-carboxylysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI5 75) chain C residue 122 type MOD_RES sequence X description N6-carboxylysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI5 76) chain D residue 122 type MOD_RES sequence X description N6-carboxylysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI5 77) chain A residue 31-41 type prosite sequence AVVKANAYGHG description ALANINE_RACEMASE Alanine racemase pyridoxal-phosphate attachment site. AVvKANAYGHG source prosite : PS00395

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