eF-site ID 3jzi-A PDB Code 3jzi Chain A 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 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 A residue 292 type ACT_SITE sequence R description ACT_SITE => ECO:0000269|PubMed:19213731 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 154-168 type prosite sequence YPVIIKASGGGGGRG description CPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVIIKASgggGGrG source prosite : PS00866 21) chain A residue 286-293 type prosite sequence FIEMNTRI description CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FIEMNTRI source prosite : PS00867 22) 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 23) 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 24) 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 25) 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 26) chain A residue 209 type BINDING sequence H description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C source Swiss-Prot : SWS_FT_FI5 27) chain A residue 238 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C source Swiss-Prot : SWS_FT_FI5 28) chain A residue 292 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C source Swiss-Prot : SWS_FT_FI5 29) chain A residue 295 type BINDING sequence V description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C source Swiss-Prot : SWS_FT_FI5 30) chain A residue 338 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C source Swiss-Prot : SWS_FT_FI5 31) 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 32) chain A residue 276 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00409 source Swiss-Prot : SWS_FT_FI7 33) chain A residue 288 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00409 source Swiss-Prot : SWS_FT_FI7 34) chain A residue 290 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00409 source Swiss-Prot : SWS_FT_FI7

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