eF-site ID 3jzi-AB PDB Code 3jzi Chain A, B click to enlarge Title Crystal structure of biotin carboxylase from E. Coli in complex with benzimidazole series Classification LIGASE Compound Biotin carboxylase Source Escherichia coli (strain K12) (ACCC_ECOLI) Sequence A:  MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLK HVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAIHP GYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAI AAMKKAGVPCVPGSDGPLGDDMDKNRAIAKRIGYPVIIKA SGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYM EKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVV EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFE NGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAGQP LSIKQEEVHVRGHAVECRINAEDPNTFLPSPGKITRFHAP GGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAIA RMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYL EKKLG B:  RHMLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRD LKHVLLADETVCIGPAPSVKSYLNIPAIISAAEITGAVAI HPGYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVS AIAAMKKAGVPCVPGSDGPLGDDMDKNRAIAKRIGYPVII KASGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMV YMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQK VVEEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFL FENGEFYFIEMNTRIQVEHPVTEMITGVDLIKEQLRIAAG QPLSIKQEEVHVRGHAVECRINAEDPNTFLPSPGKITRFH APGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVA IARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIH YLEKKL Description Functional site 1) chain A residue 116 type sequence K description BINDING SITE FOR RESIDUE JZL A 466 source : AC1 2) chain A residue 159 type sequence K description BINDING SITE FOR RESIDUE JZL A 466 source : AC1 3) chain A residue 160 type sequence A description BINDING SITE FOR RESIDUE JZL A 466 source : AC1 4) chain A residue 164 type sequence G description BINDING SITE FOR RESIDUE JZL A 466 source : AC1 5) chain A residue 165 type sequence G description BINDING SITE FOR RESIDUE JZL A 466 source : AC1 6) chain A residue 167 type sequence R description BINDING SITE FOR RESIDUE JZL A 466 source : AC1 7) chain A residue 169 type sequence M description BINDING SITE FOR RESIDUE JZL A 466 source : AC1 8) chain A residue 199 type sequence Y description BINDING SITE FOR RESIDUE JZL A 466 source : AC1 9) chain A residue 201 type sequence E description BINDING SITE FOR RESIDUE JZL A 466 source : AC1 10) chain A residue 202 type sequence K description BINDING SITE FOR RESIDUE JZL A 466 source : AC1 11) chain A residue 203 type sequence Y description BINDING SITE FOR RESIDUE JZL A 466 source : AC1 12) chain A residue 204 type sequence L description BINDING SITE FOR RESIDUE JZL A 466 source : AC1 13) chain A residue 209 type sequence H description BINDING SITE FOR RESIDUE JZL A 466 source : AC1 14) chain A residue 233 type sequence Q description BINDING SITE FOR RESIDUE JZL A 466 source : AC1 15) chain A residue 236 type sequence H description BINDING SITE FOR RESIDUE JZL A 466 source : AC1 16) chain A residue 278 type sequence L description BINDING SITE FOR RESIDUE JZL A 466 source : AC1 17) chain A residue 287 type sequence I description BINDING SITE FOR RESIDUE JZL A 466 source : AC1 18) chain A residue 288 type sequence E description BINDING SITE FOR RESIDUE JZL A 466 source : AC1 19) chain B residue 116 type sequence K description BINDING SITE FOR RESIDUE JZL B 466 source : AC2 20) chain B residue 157 type sequence I description BINDING SITE FOR RESIDUE JZL B 466 source : AC2 21) chain B residue 159 type sequence K description BINDING SITE FOR RESIDUE JZL B 466 source : AC2 22) chain B residue 160 type sequence A description BINDING SITE FOR RESIDUE JZL B 466 source : AC2 23) chain B residue 164 type sequence G description BINDING SITE FOR RESIDUE JZL B 466 source : AC2 24) chain B residue 165 type sequence G description BINDING SITE FOR RESIDUE JZL B 466 source : AC2 25) chain B residue 167 type sequence R description BINDING SITE FOR RESIDUE JZL B 466 source : AC2 26) chain B residue 168 type sequence G description BINDING SITE FOR RESIDUE JZL B 466 source : AC2 27) chain B residue 169 type sequence M description BINDING SITE FOR RESIDUE JZL B 466 source : AC2 28) chain B residue 199 type sequence Y description BINDING SITE FOR RESIDUE JZL B 466 source : AC2 29) chain B residue 201 type sequence E description BINDING SITE FOR RESIDUE JZL B 466 source : AC2 30) chain B residue 202 type sequence K description BINDING SITE FOR RESIDUE JZL B 466 source : AC2 31) chain B residue 203 type sequence Y description BINDING SITE FOR RESIDUE JZL B 466 source : AC2 32) chain B residue 204 type sequence L description BINDING SITE FOR RESIDUE JZL B 466 source : AC2 33) chain B residue 209 type sequence H description BINDING SITE FOR RESIDUE JZL B 466 source : AC2 34) chain B residue 233 type sequence Q description BINDING SITE FOR RESIDUE JZL B 466 source : AC2 35) chain B residue 236 type sequence H description BINDING SITE FOR RESIDUE JZL B 466 source : AC2 36) chain B residue 278 type sequence L description BINDING SITE FOR RESIDUE JZL B 466 source : AC2 37) chain B residue 287 type sequence I description BINDING SITE FOR RESIDUE JZL B 466 source : AC2 38) chain B residue 288 type sequence E description BINDING SITE FOR RESIDUE JZL B 466 source : AC2 39) chain A residue 154-168 type prosite sequence YPVIIKASGGGGGRG description CPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVIIKASgggGGrG source prosite : PS00866 40) chain A residue 286-293 type prosite sequence FIEMNTRI description CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FIEMNTRI source prosite : PS00867 41) chain A residue 292 type ACT_SITE sequence R description ACT_SITE => ECO:0000269|PubMed:19213731 source Swiss-Prot : SWS_FT_FI1 42) chain B residue 292 type ACT_SITE sequence R description ACT_SITE => ECO:0000269|PubMed:19213731 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 116 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8D source Swiss-Prot : SWS_FT_FI2 44) chain A residue 165 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8D source Swiss-Prot : SWS_FT_FI2 45) chain B residue 116 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8D source Swiss-Prot : SWS_FT_FI2 46) chain B residue 165 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8D source Swiss-Prot : SWS_FT_FI2 47) chain A residue 159 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D source Swiss-Prot : SWS_FT_FI3 48) chain B residue 159 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D source Swiss-Prot : SWS_FT_FI3 49) chain A residue 201 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D source Swiss-Prot : SWS_FT_FI4 50) chain B residue 201 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D source Swiss-Prot : SWS_FT_FI4 51) chain A residue 209 type BINDING sequence H description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C source Swiss-Prot : SWS_FT_FI5 52) chain B residue 338 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C source Swiss-Prot : SWS_FT_FI5 53) chain A residue 238 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C source Swiss-Prot : SWS_FT_FI5 54) chain A residue 292 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C source Swiss-Prot : SWS_FT_FI5 55) chain A residue 295 type BINDING sequence V description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C source Swiss-Prot : SWS_FT_FI5 56) chain A residue 338 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C source Swiss-Prot : SWS_FT_FI5 57) chain B residue 209 type BINDING sequence H description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C source Swiss-Prot : SWS_FT_FI5 58) chain B residue 238 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C source Swiss-Prot : SWS_FT_FI5 59) chain B residue 292 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C source Swiss-Prot : SWS_FT_FI5 60) chain B residue 295 type BINDING sequence V description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C source Swiss-Prot : SWS_FT_FI5 61) chain A residue 236 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8C source Swiss-Prot : SWS_FT_FI6 62) chain B residue 236 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8C source Swiss-Prot : SWS_FT_FI6 63) chain A residue 276 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00409 source Swiss-Prot : SWS_FT_FI7 64) chain A residue 288 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00409 source Swiss-Prot : SWS_FT_FI7 65) chain A residue 290 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00409 source Swiss-Prot : SWS_FT_FI7 66) chain B residue 276 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00409 source Swiss-Prot : SWS_FT_FI7 67) chain B residue 288 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00409 source Swiss-Prot : SWS_FT_FI7 68) chain B residue 290 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00409 source Swiss-Prot : SWS_FT_FI7

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