eF-site ID 3b8v-ABCD PDB Code 3b8v Chain A, B, C, D click to enlarge Title Crystal structure of Escherichia coli alaine racemase mutant E221K Classification ISOMERASE Compound Alanine racemase Source null (ALR1_ECOLI) Sequence A:  MQAATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGH GLLETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEG FFDARDLPTISAQHFHTAVHNEEQLAALEEASLDEPVTVW MXLDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHF ARADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLW PQSHFDWVRPGIILYGVSPLKDRSTGADFGCQPVMSLTSS LIAVREHKAGEPVGYGGTWVSERDTRLGVVAMGYGDGYPR AAPSGTPVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGD PVILWGEGLPVERIAEMTKVSAYELITRLTSRVAMKYVD B:  MQAATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGH GLLETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEG FFDARDLPTISAQHFHTAVHNEEQLAALEEASLDEPVTVW MXLDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHF ARADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLW PQSHFDWVRPGIILYGVSPLKDRSTGADFGCQPVMSLTSS LIAVREHKAGEPVGYGGTWVSERDTRLGVVAMGYGDGYPR AAPSGTPVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGD PVILWGEGLPVERIAEMTKVSAYELITRLTSRVAMKYVD C:  AATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGHGL LETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEGFF DARDLPTISAQHFHTAVHNEEQLAALEEASLDEPVTVWMX LDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHFAR ADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLWPQ SHFDWVRPGIILYGVSPLKDRSTGADFGCQPVMSLTSSLI AVREHKAGEPVGYGGTWVSERDTRLGVVAMGYGDGYPRAA PSGTPVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGDPV ILWGEGLPVERIMTKVSAYELITRLTSRVAMKYVD D:  AATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGHGL LETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEGFF DARDLPTISAQHFHTAVHNEEQLAALEEASLDEPVTVWMX LDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHFAR ADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLWPQ SHFDWVRPGIILYGVSPLKDRSTGADFGCQPVMSLTSSLI AVREHKAGEPVGYGGTWVSERDTRLGVVAMGYGDGYPRAA PSGTPVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGDPV ILWGEGLPVERIKVSAYELITRLTSRVAMKYVD Description Functional site 1) chain A residue 255 type sequence Y description BINDING SITE FOR RESIDUE SO4 A 360 source : AC1 2) chain A residue 274 type sequence Y description BINDING SITE FOR RESIDUE SO4 A 360 source : AC1 3) chain A residue 280 type sequence R description BINDING SITE FOR RESIDUE SO4 A 360 source : AC1 4) chain B residue 343 type sequence Y description BINDING SITE FOR RESIDUE SO4 A 360 source : AC1 5) chain A residue 19 type sequence R description BINDING SITE FOR RESIDUE SO4 A 361 source : AC2 6) chain B residue 266 type sequence R description BINDING SITE FOR RESIDUE SO4 A 361 source : AC2 7) chain A residue 162 type sequence R description BINDING SITE FOR RESIDUE SO4 A 362 source : AC3 8) chain A residue 343 type sequence Y description BINDING SITE FOR RESIDUE SO4 B 360 source : AC4 9) chain B residue 255 type sequence Y description BINDING SITE FOR RESIDUE SO4 B 360 source : AC4 10) chain B residue 274 type sequence Y description BINDING SITE FOR RESIDUE SO4 B 360 source : AC4 11) chain B residue 280 type sequence R description BINDING SITE FOR RESIDUE SO4 B 360 source : AC4 12) chain A residue 266 type sequence R description BINDING SITE FOR RESIDUE SO4 B 361 source : AC5 13) chain B residue 19 type sequence R description BINDING SITE FOR RESIDUE SO4 B 361 source : AC5 14) chain C residue 255 type sequence Y description BINDING SITE FOR RESIDUE SO4 C 360 source : AC6 15) chain C residue 274 type sequence Y description BINDING SITE FOR RESIDUE SO4 C 360 source : AC6 16) chain C residue 302 type sequence A description BINDING SITE FOR RESIDUE SO4 C 360 source : AC6 17) chain C residue 19 type sequence R description BINDING SITE FOR RESIDUE SO4 C 361 source : AC7 18) chain D residue 266 type sequence R description BINDING SITE FOR RESIDUE SO4 C 361 source : AC7 19) chain D residue 314 type sequence A description BINDING SITE FOR RESIDUE SO4 C 361 source : AC7 20) chain C residue 162 type sequence R description BINDING SITE FOR RESIDUE SO4 C 362 source : AC8 21) chain C residue 168 type sequence C description BINDING SITE FOR RESIDUE SO4 C 362 source : AC8 22) chain A residue 280 type sequence R description BINDING SITE FOR RESIDUE SO4 A 363 source : AC9 23) chain A residue 300 type sequence R description BINDING SITE FOR RESIDUE SO4 A 363 source : AC9 24) chain B residue 221 type sequence K description BINDING SITE FOR RESIDUE SO4 A 363 source : AC9 25) chain A residue 221 type sequence K description BINDING SITE FOR RESIDUE SO4 B 363 source : BC1 26) chain B residue 280 type sequence R description BINDING SITE FOR RESIDUE SO4 B 363 source : BC1 27) chain B residue 300 type sequence R description BINDING SITE FOR RESIDUE SO4 B 363 source : BC1 28) chain A residue 34 type sequence K description BINDING SITE FOR RESIDUE PLP A 1001 source : BC2 29) chain A residue 38 type sequence Y description BINDING SITE FOR RESIDUE PLP A 1001 source : BC2 30) chain A residue 159 type sequence H description BINDING SITE FOR RESIDUE PLP A 1001 source : BC2 31) chain A residue 193 type sequence A description BINDING SITE FOR RESIDUE PLP A 1001 source : BC2 32) chain A residue 194 type sequence S description BINDING SITE FOR RESIDUE PLP A 1001 source : BC2 33) chain A residue 209 type sequence R description BINDING SITE FOR RESIDUE PLP A 1001 source : BC2 34) chain A residue 211 type sequence G description BINDING SITE FOR RESIDUE PLP A 1001 source : BC2 35) chain A residue 212 type sequence I description BINDING SITE FOR RESIDUE PLP A 1001 source : BC2 36) chain A residue 343 type sequence Y description BINDING SITE FOR RESIDUE PLP A 1001 source : BC2 37) chain B residue 34 type sequence K description BINDING SITE FOR RESIDUE PLP B 1001 source : BC3 38) chain B residue 38 type sequence Y description BINDING SITE FOR RESIDUE PLP B 1001 source : BC3 39) chain B residue 159 type sequence H description BINDING SITE FOR RESIDUE PLP B 1001 source : BC3 40) chain B residue 193 type sequence A description BINDING SITE FOR RESIDUE PLP B 1001 source : BC3 41) chain B residue 194 type sequence S description BINDING SITE FOR RESIDUE PLP B 1001 source : BC3 42) chain B residue 209 type sequence R description BINDING SITE FOR RESIDUE PLP B 1001 source : BC3 43) chain B residue 211 type sequence G description BINDING SITE FOR RESIDUE PLP B 1001 source : BC3 44) chain B residue 212 type sequence I description BINDING SITE FOR RESIDUE PLP B 1001 source : BC3 45) chain B residue 343 type sequence Y description BINDING SITE FOR RESIDUE PLP B 1001 source : BC3 46) chain C residue 34 type sequence K description BINDING SITE FOR RESIDUE PLP C 1001 source : BC4 47) chain C residue 38 type sequence Y description BINDING SITE FOR RESIDUE PLP C 1001 source : BC4 48) chain C residue 78 type sequence L description BINDING SITE FOR RESIDUE PLP C 1001 source : BC4 49) chain C residue 159 type sequence H description BINDING SITE FOR RESIDUE PLP C 1001 source : BC4 50) chain C residue 193 type sequence A description BINDING SITE FOR RESIDUE PLP C 1001 source : BC4 51) chain C residue 194 type sequence S description BINDING SITE FOR RESIDUE PLP C 1001 source : BC4 52) chain C residue 209 type sequence R description BINDING SITE FOR RESIDUE PLP C 1001 source : BC4 53) chain C residue 211 type sequence G description BINDING SITE FOR RESIDUE PLP C 1001 source : BC4 54) chain C residue 212 type sequence I description BINDING SITE FOR RESIDUE PLP C 1001 source : BC4 55) chain C residue 343 type sequence Y description BINDING SITE FOR RESIDUE PLP C 1001 source : BC4 56) chain D residue 34 type sequence K description BINDING SITE FOR RESIDUE PLP D 1001 source : BC5 57) chain D residue 38 type sequence Y description BINDING SITE FOR RESIDUE PLP D 1001 source : BC5 58) chain D residue 159 type sequence H description BINDING SITE FOR RESIDUE PLP D 1001 source : BC5 59) chain D residue 193 type sequence A description BINDING SITE FOR RESIDUE PLP D 1001 source : BC5 60) chain D residue 194 type sequence S description BINDING SITE FOR RESIDUE PLP D 1001 source : BC5 61) chain D residue 209 type sequence R description BINDING SITE FOR RESIDUE PLP D 1001 source : BC5 62) chain D residue 211 type sequence G description BINDING SITE FOR RESIDUE PLP D 1001 source : BC5 63) chain D residue 212 type sequence I description BINDING SITE FOR RESIDUE PLP D 1001 source : BC5 64) chain D residue 343 type sequence Y description BINDING SITE FOR RESIDUE PLP D 1001 source : BC5 65) 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 66) 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 67) 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 68) 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 69) 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 70) 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 71) 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 72) 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 73) chain A residue 129 type BINDING sequence R description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 74) chain A residue 303 type BINDING sequence M description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 75) chain B residue 129 type BINDING sequence R description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 76) chain B residue 303 type BINDING sequence M description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 77) chain C residue 129 type BINDING sequence R description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 78) chain C residue 303 type BINDING sequence M description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 79) chain D residue 129 type BINDING sequence R description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 80) chain D residue 303 type BINDING sequence M description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 81) chain A residue 34 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI4 82) chain B residue 34 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI4 83) chain C residue 34 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI4 84) chain D residue 34 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI4 85) chain A residue 122 type MOD_RES sequence X description N6-carboxylysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI5 86) chain B residue 122 type MOD_RES sequence X description N6-carboxylysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI5 87) chain C residue 122 type MOD_RES sequence X description N6-carboxylysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI5 88) chain D residue 122 type MOD_RES sequence X description N6-carboxylysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI5 89) 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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