eF-site ID 3b8u-ABCD PDB Code 3b8u Chain A, B, C, D click to enlarge Title Crystal structure of Escherichia coli alaine racemase mutant E221A Classification ISOMERASE Compound Alanine racemase Source Escherichia coli (strain K12) (ALR1_ECOLI) Sequence A:  MQAATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGH GLLETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEG FFDARDLPTISAQHFHTAVHNEEQLAALEEASLDEPVTVW MXLDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHF ARADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLW PQSHFDWVRPGIILYGVSPLADRSTGADFGCQPVMSLTSS LIAVREHKAGEPVGYGGTWVSERDTRLGVVAMGYGDGYPR AAPSGTPVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGD PVILWGEGLPVERIAEMTKVSAYELITRLTSRVAMKYVD B:  QAATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGHG LLETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEGF FDARDLPTISAQHFHTAVHNEEQLAALEEASLDEPVTVWM XLDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHFA RADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLWP QSHFDWVRPGIILYGVSPLADRSTGADFGCQPVMSLTSSL IAVREHKAGEPVGYGGTWVSERDTRLGVVAMGYGDGYPRA APSGTPVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGDP VILWGEGLPVERIAEMTKVSAYELITRLTSRVAMKYVD C:  AATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGHGL LETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEGFF DARDLPTISAQHFHTAVHNEEQLAALEEASLDEPVTVWMX LDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHFAR ADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLWPQ SHFDWVRPGIILYGVSPLADRSTGADFGCQPVMSLTSSLI AVREHKAGEPVGYGGTWVSERDTRLGVVAMGYGDGYPRAA PSGTPVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGDPV ILWLPVERIKVSAYELITRLTSRVAMKYVD D:  AATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGHGL LETARTLPDADAFGVARLEEALRLRAGGITKPVLLLEGFF DARDLPTISAQHFHTAVHNEEQLAALEEALDEPVTVWMXL DTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVNIVSHFARA DEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLWPQS HFDWVRPGIILYGVSPLSTGADFGCQPVMSLTSSLIAVRE HKAGEPVGYGGTWVSERDTRLGVVAMGYGDGYPRAAPSGT PVLVNGREVPIVGRVAMDMICVDLGPQAQDKAGDPVILWG EGLPVERIKVSAYELITRLTSRVAMKYVD 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 A residue 19 type sequence R description BINDING SITE FOR RESIDUE SO4 A 361 source : AC2 5) chain B residue 266 type sequence R description BINDING SITE FOR RESIDUE SO4 A 361 source : AC2 6) chain B residue 315 type sequence Q description BINDING SITE FOR RESIDUE SO4 A 361 source : AC2 7) chain B residue 255 type sequence Y description BINDING SITE FOR RESIDUE SO4 B 360 source : AC3 8) chain B residue 274 type sequence Y description BINDING SITE FOR RESIDUE SO4 B 360 source : AC3 9) chain B residue 280 type sequence R description BINDING SITE FOR RESIDUE SO4 B 360 source : AC3 10) chain A residue 266 type sequence R description BINDING SITE FOR RESIDUE SO4 B 361 source : AC4 11) chain B residue 19 type sequence R description BINDING SITE FOR RESIDUE SO4 B 361 source : AC4 12) chain B residue 162 type sequence R description BINDING SITE FOR RESIDUE SO4 B 362 source : AC5 13) chain C residue 255 type sequence Y description BINDING SITE FOR RESIDUE SO4 C 360 source : AC6 14) chain C residue 274 type sequence Y description BINDING SITE FOR RESIDUE SO4 C 360 source : AC6 15) chain C residue 280 type sequence R 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 C residue 343 type sequence Y description BINDING SITE FOR RESIDUE SO4 D 360 source : AC8 20) chain D residue 255 type sequence Y description BINDING SITE FOR RESIDUE SO4 D 360 source : AC8 21) chain D residue 274 type sequence Y description BINDING SITE FOR RESIDUE SO4 D 360 source : AC8 22) chain D residue 280 type sequence R description BINDING SITE FOR RESIDUE SO4 D 360 source : AC8 23) chain C residue 266 type sequence R description BINDING SITE FOR RESIDUE SO4 D 361 source : AC9 24) chain D residue 19 type sequence R description BINDING SITE FOR RESIDUE SO4 D 361 source : AC9 25) chain A residue 34 type sequence K description BINDING SITE FOR RESIDUE PLP A 1001 source : BC1 26) chain A residue 38 type sequence Y description BINDING SITE FOR RESIDUE PLP A 1001 source : BC1 27) chain A residue 159 type sequence H description BINDING SITE FOR RESIDUE PLP A 1001 source : BC1 28) chain A residue 193 type sequence A description BINDING SITE FOR RESIDUE PLP A 1001 source : BC1 29) chain A residue 194 type sequence S description BINDING SITE FOR RESIDUE PLP A 1001 source : BC1 30) chain A residue 209 type sequence R description BINDING SITE FOR RESIDUE PLP A 1001 source : BC1 31) chain A residue 211 type sequence G description BINDING SITE FOR RESIDUE PLP A 1001 source : BC1 32) chain A residue 212 type sequence I description BINDING SITE FOR RESIDUE PLP A 1001 source : BC1 33) chain A residue 343 type sequence Y description BINDING SITE FOR RESIDUE PLP A 1001 source : BC1 34) chain B residue 34 type sequence K description BINDING SITE FOR RESIDUE PLP B 1001 source : BC2 35) chain B residue 38 type sequence Y description BINDING SITE FOR RESIDUE PLP B 1001 source : BC2 36) chain B residue 159 type sequence H description BINDING SITE FOR RESIDUE PLP B 1001 source : BC2 37) chain B residue 193 type sequence A description BINDING SITE FOR RESIDUE PLP B 1001 source : BC2 38) chain B residue 194 type sequence S description BINDING SITE FOR RESIDUE PLP B 1001 source : BC2 39) chain B residue 209 type sequence R description BINDING SITE FOR RESIDUE PLP B 1001 source : BC2 40) chain B residue 211 type sequence G description BINDING SITE FOR RESIDUE PLP B 1001 source : BC2 41) chain B residue 212 type sequence I description BINDING SITE FOR RESIDUE PLP B 1001 source : BC2 42) chain B residue 343 type sequence Y description BINDING SITE FOR RESIDUE PLP B 1001 source : BC2 43) chain C residue 34 type sequence K description BINDING SITE FOR RESIDUE PLP C 1001 source : BC3 44) chain C residue 38 type sequence Y description BINDING SITE FOR RESIDUE PLP C 1001 source : BC3 45) chain C residue 78 type sequence L description BINDING SITE FOR RESIDUE PLP C 1001 source : BC3 46) chain C residue 159 type sequence H description BINDING SITE FOR RESIDUE PLP C 1001 source : BC3 47) chain C residue 193 type sequence A description BINDING SITE FOR RESIDUE PLP C 1001 source : BC3 48) chain C residue 194 type sequence S description BINDING SITE FOR RESIDUE PLP C 1001 source : BC3 49) chain C residue 209 type sequence R description BINDING SITE FOR RESIDUE PLP C 1001 source : BC3 50) chain C residue 211 type sequence G description BINDING SITE FOR RESIDUE PLP C 1001 source : BC3 51) chain C residue 212 type sequence I description BINDING SITE FOR RESIDUE PLP C 1001 source : BC3 52) chain C residue 343 type sequence Y description BINDING SITE FOR RESIDUE PLP C 1001 source : BC3 53) chain D residue 34 type sequence K description BINDING SITE FOR RESIDUE PLP D 1001 source : BC4 54) chain D residue 38 type sequence Y description BINDING SITE FOR RESIDUE PLP D 1001 source : BC4 55) chain D residue 159 type sequence H description BINDING SITE FOR RESIDUE PLP D 1001 source : BC4 56) chain D residue 193 type sequence A description BINDING SITE FOR RESIDUE PLP D 1001 source : BC4 57) chain D residue 194 type sequence S description BINDING SITE FOR RESIDUE PLP D 1001 source : BC4 58) chain D residue 209 type sequence R description BINDING SITE FOR RESIDUE PLP D 1001 source : BC4 59) chain D residue 211 type sequence G description BINDING SITE FOR RESIDUE PLP D 1001 source : BC4 60) chain D residue 212 type sequence I description BINDING SITE FOR RESIDUE PLP D 1001 source : BC4 61) chain D residue 343 type sequence Y description BINDING SITE FOR RESIDUE PLP D 1001 source : BC4 62) chain A residue 31-41 type prosite sequence AVVKANAYGHG description ALANINE_RACEMASE Alanine racemase pyridoxal-phosphate attachment site. AVvKANAYGHG source prosite : PS00395 63) 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 64) 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 65) 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 66) 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 67) 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 68) 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 69) 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 70) 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 71) chain A residue 129 type BINDING sequence R description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 72) chain A residue 303 type BINDING sequence M description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 73) chain B residue 129 type BINDING sequence R description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 74) chain B residue 303 type BINDING sequence M description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 75) chain C residue 129 type BINDING sequence R description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 76) chain C residue 303 type BINDING sequence M description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 77) chain D residue 129 type BINDING sequence R description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 78) chain D residue 303 type BINDING sequence M description BINDING => ECO:0000305|PubMed:18434499 source Swiss-Prot : SWS_FT_FI3 79) chain A residue 34 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI4 80) chain B residue 34 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI4 81) chain C residue 34 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI4 82) chain D residue 34 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI4 83) chain A residue 122 type MOD_RES sequence X description N6-carboxylysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI5 84) chain B residue 122 type MOD_RES sequence X description N6-carboxylysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI5 85) chain C residue 122 type MOD_RES sequence X description N6-carboxylysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI5 86) chain D residue 122 type MOD_RES sequence X description N6-carboxylysine => ECO:0000269|PubMed:18434499 source Swiss-Prot : SWS_FT_FI5

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