eF-site ID 4o9c-ABCDEFGH PDB Code 4o9c Chain A, B, C, D, E, F, G, H click to enlarge Title Crystal structure of Beta-ketothiolase (PhaA) from Ralstonia eutropha H16 Classification TRANSFERASE Compound Acetyl-CoA acetyltransferase Source Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) (THIL_CUPNH) Sequence A:  MTDVVIVSAARTAVGKFGGSLAKIPAPELGAVVIKAALER AGVKPEQVSEVIMGQVLTAGSGQNPARQAAIKAGLPAMVP AMTINKVSGSGLKAVMLAANAIMAGDAEIVVAGGQENMSA APHVLPGSRDGFRMGDAKLVDTMIVDGLWDVYNQYHMGIT AENVAKEYGITREAQDEFAVGSQNKAEAAQKAGKFDEEIV PVLIPQRKGDPVAFKTDEFVRQGATLDSMSGLKPAFDKAG TVTAANASGLNDGAAAVVVMSAAKAKELGLTPLATIKSYA NAGVDPKVMGMGPVPASKRALSRAEWTPQDLDLMEINEAF AAQALAVHQQMGWDTSKVNVNGGAIAIGHPIGASGCRILV TLLHEMKRRDAKKGLASLCIGGGMGVALAVERK B:  MTDVVIVSAARTAVGKFGGSLAKIPAPELGAVVIKAALER AGVKPEQVSEVIMGQVLTAGSGQNPARQAAIKAGLPAMVP AMTINKVSGSGLKAVMLAANAIMAGDAEIVVAGGQENMSA APHVLPGSRDGFRMGDAKLVDTMIVDGLWDVYNQYHMGIT AENVAKEYGITREAQDEFAVGSQNKAEAAQKAGKFDEEIV PVLIPQRKGDPVAFKTDEFVRQGATLDSMSGLKPAFDKAG TVTAANASGLNDGAAAVVVMSAAKAKELGLTPLATIKSYA NAGVDPKVMGMGPVPASKRALSRAEWTPQDLDLMEINEAF AAQALAVHQQMGWDTSKVNVNGGAIAIGHPIGASGCRILV TLLHEMKRRDAKKGLASLCIGGGMGVALAVERK C:  MTDVVIVSAARTAVGKFGGSLAKIPAPELGAVVIKAALER AGVKPEQVSEVIMGQVLTAGSGQNPARQAAIKAGLPAMVP AMTINKVSGSGLKAVMLAANAIMAGDAEIVVAGGQENMSA APHVLPGSRDGFRMGDAKLVDTMIVDGLWDVYNQYHMGIT AENVAKEYGITREAQDEFAVGSQNKAEAAQKAGKFDEEIV PVLIPQRKGDPVAFKTDEFVRQGATLDSMSGLKPAFDKAG TVTAANASGLNDGAAAVVVMSAAKAKELGLTPLATIKSYA NAGVDPKVMGMGPVPASKRALSRAEWTPQDLDLMEINEAF AAQALAVHQQMGWDTSKVNVNGGAIAIGHPIGASGCRILV TLLHEMKRRDAKKGLASLCIGGGMGVALAVERK D:  MTDVVIVSAARTAVGKFGGSLAKIPAPELGAVVIKAALER AGVKPEQVSEVIMGQVLTAGSGQNPARQAAIKAGLPAMVP AMTINKVSGSGLKAVMLAANAIMAGDAEIVVAGGQENMSA APHVLPGSRDGFRMGDAKLVDTMIVDGLWDVYNQYHMGIT AENVAKEYGITREAQDEFAVGSQNKAEAAQKAGKFDEEIV PVLIPQRKGDPVAFKTDEFVRQGATLDSMSGLKPAFDKAG TVTAANASGLNDGAAAVVVMSAAKAKELGLTPLATIKSYA NAGVDPKVMGMGPVPASKRALSRAEWTPQDLDLMEINEAF AAQALAVHQQMGWDTSKVNVNGGAIAIGHPIGASGCRILV TLLHEMKRRDAKKGLASLCIGGGMGVALAVERK E:  MTDVVIVSAARTAVGKFGGSLAKIPAPELGAVVIKAALER AGVKPEQVSEVIMGQVLTAGSGQNPARQAAIKAGLPAMVP AMTINKVSGSGLKAVMLAANAIMAGDAEIVVAGGQENMSA APHVLPGSRDGFRMGDAKLVDTMIVDGLWDVYNQYHMGIT AENVAKEYGITREAQDEFAVGSQNKAEAAQKAGKFDEEIV PVLIPQRKGDPVAFKTDEFVRQGATLDSMSGLKPAFDKAG TVTAANASGLNDGAAAVVVMSAAKAKELGLTPLATIKSYA NAGVDPKVMGMGPVPASKRALSRAEWTPQDLDLMEINEAF AAQALAVHQQMGWDTSKVNVNGGAIAIGHPIGASGCRILV TLLHEMKRRDAKKGLASLCIGGGMGVALAVERK F:  MTDVVIVSAARTAVGKFGGSLAKIPAPELGAVVIKAALER AGVKPEQVSEVIMGQVLTAGSGQNPARQAAIKAGLPAMVP AMTINKVSGSGLKAVMLAANAIMAGDAEIVVAGGQENMSA APHVLPGSRDGFRMGDAKLVDTMIVDGLWDVYNQYHMGIT AENVAKEYGITREAQDEFAVGSQNKAEAAQKAGKFDEEIV PVLIPQRKGDPVAFKTDEFVRQGATLDSMSGLKPAFDKAG TVTAANASGLNDGAAAVVVMSAAKAKELGLTPLATIKSYA NAGVDPKVMGMGPVPASKRALSRAEWTPQDLDLMEINEAF AAQALAVHQQMGWDTSKVNVNGGAIAIGHPIGASGCRILV TLLHEMKRRDAKKGLASLCIGGGMGVALAVERK G:  MTDVVIVSAARTAVGKFGGSLAKIPAPELGAVVIKAALER AGVKPEQVSEVIMGQVLTAGSGQNPARQAAIKAGLPAMVP AMTINKVSGSGLKAVMLAANAIMAGDAEIVVAGGQENMSA APHVLPGSRDGFRMGDAKLVDTMIVDGLWDVYNQYHMGIT AENVAKEYGITREAQDEFAVGSQNKAEAAQKAGKFDEEIV PVLIPQRKGDPVAFKTDEFVRQGATLDSMSGLKPAFDKAG TVTAANASGLNDGAAAVVVMSAAKAKELGLTPLATIKSYA NAGVDPKVMGMGPVPASKRALSRAEWTPQDLDLMEINEAF AAQALAVHQQMGWDTSKVNVNGGAIAIGHPIGASGCRILV TLLHEMKRRDAKKGLASLCIGGGMGVALAVERK H:  MTDVVIVSAARTAVGKFGGSLAKIPAPELGAVVIKAALER AGVKPEQVSEVIMGQVLTAGSGQNPARQAAIKAGLPAMVP AMTINKVSGSGLKAVMLAANAIMAGDAEIVVAGGQENMSA APHVLPGSRDGFRMGDAKLVDTMIVDGLWDVYNQYHMGIT AENVAKEYGITREAQDEFAVGSQNKAEAAQKAGKFDEEIV PVLIPQRKGDPVAFKTDEFVRQGATLDSMSGLKPAFDKAG TVTAANASGLNDGAAAVVVMSAAKAKELGLTPLATIKSYA NAGVDPKVMGMGPVPASKRALSRAEWTPQDLDLMEINEAF AAQALAVHQQMGWDTSKVNVNGGAIAIGHPIGASGCRILV TLLHEMKRRDAKKGLASLCIGGGMGVALAVERK Description Functional site 1) chain C residue 88 type sequence S description BINDING SITE FOR RESIDUE COA C 401 source : AC1 2) chain C residue 148 type sequence L description BINDING SITE FOR RESIDUE COA C 401 source : AC1 3) chain C residue 156 type sequence H description BINDING SITE FOR RESIDUE COA C 401 source : AC1 4) chain C residue 221 type sequence R description BINDING SITE FOR RESIDUE COA C 401 source : AC1 5) chain C residue 236 type sequence F description BINDING SITE FOR RESIDUE COA C 401 source : AC1 6) chain C residue 244 type sequence A description BINDING SITE FOR RESIDUE COA C 401 source : AC1 7) chain C residue 248 type sequence S description BINDING SITE FOR RESIDUE COA C 401 source : AC1 8) chain C residue 249 type sequence G description BINDING SITE FOR RESIDUE COA C 401 source : AC1 9) chain C residue 250 type sequence L description BINDING SITE FOR RESIDUE COA C 401 source : AC1 10) chain C residue 319 type sequence A description BINDING SITE FOR RESIDUE COA C 401 source : AC1 11) chain C residue 320 type sequence F description BINDING SITE FOR RESIDUE COA C 401 source : AC1 12) chain C residue 349 type sequence H description BINDING SITE FOR RESIDUE COA C 401 source : AC1 13) chain H residue 134 type sequence M description BINDING SITE FOR RESIDUE COA C 401 source : AC1 14) chain B residue 349 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000305|PubMed:25152395 source Swiss-Prot : SWS_FT_FI2 15) chain B residue 379 type ACT_SITE sequence C description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000305|PubMed:25152395 source Swiss-Prot : SWS_FT_FI2 16) chain C residue 349 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000305|PubMed:25152395 source Swiss-Prot : SWS_FT_FI2 17) chain C residue 379 type ACT_SITE sequence C description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000305|PubMed:25152395 source Swiss-Prot : SWS_FT_FI2 18) chain D residue 349 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000305|PubMed:25152395 source Swiss-Prot : SWS_FT_FI2 19) chain D residue 379 type ACT_SITE sequence C description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000305|PubMed:25152395 source Swiss-Prot : SWS_FT_FI2 20) chain E residue 349 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000305|PubMed:25152395 source Swiss-Prot : SWS_FT_FI2 21) chain E residue 379 type ACT_SITE sequence C description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000305|PubMed:25152395 source Swiss-Prot : SWS_FT_FI2 22) chain F residue 349 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000305|PubMed:25152395 source Swiss-Prot : SWS_FT_FI2 23) chain F residue 379 type ACT_SITE sequence C description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000305|PubMed:25152395 source Swiss-Prot : SWS_FT_FI2 24) chain G residue 349 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000305|PubMed:25152395 source Swiss-Prot : SWS_FT_FI2 25) chain G residue 379 type ACT_SITE sequence C description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000305|PubMed:25152395 source Swiss-Prot : SWS_FT_FI2 26) chain H residue 349 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000305|PubMed:25152395 source Swiss-Prot : SWS_FT_FI2 27) chain H residue 379 type ACT_SITE sequence C description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000305|PubMed:25152395 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 349 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000305|PubMed:25152395 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 379 type ACT_SITE sequence C description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000305|PubMed:25152395 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 374-387 type prosite sequence GLASLCIGGGMGVA description THIOLASE_3 Thiolases active site. GLASLCIGgGmGvA source prosite : PS00099 31) chain A residue 339-355 type prosite sequence NVNGGAIAIGHPIGASG description THIOLASE_2 Thiolases signature 2. NvnGGaIAiGHPiGaSG source prosite : PS00737 32) chain A residue 88 type ACT_SITE sequence S description Acyl-thioester intermediate => ECO:0000269|PubMed:25152395 source Swiss-Prot : SWS_FT_FI1 33) chain B residue 88 type ACT_SITE sequence S description Acyl-thioester intermediate => ECO:0000269|PubMed:25152395 source Swiss-Prot : SWS_FT_FI1 34) chain C residue 88 type ACT_SITE sequence S description Acyl-thioester intermediate => ECO:0000269|PubMed:25152395 source Swiss-Prot : SWS_FT_FI1 35) chain D residue 88 type ACT_SITE sequence S description Acyl-thioester intermediate => ECO:0000269|PubMed:25152395 source Swiss-Prot : SWS_FT_FI1 36) chain E residue 88 type ACT_SITE sequence S description Acyl-thioester intermediate => ECO:0000269|PubMed:25152395 source Swiss-Prot : SWS_FT_FI1 37) chain F residue 88 type ACT_SITE sequence S description Acyl-thioester intermediate => ECO:0000269|PubMed:25152395 source Swiss-Prot : SWS_FT_FI1 38) chain G residue 88 type ACT_SITE sequence S description Acyl-thioester intermediate => ECO:0000269|PubMed:25152395 source Swiss-Prot : SWS_FT_FI1 39) chain H residue 88 type ACT_SITE sequence S description Acyl-thioester intermediate => ECO:0000269|PubMed:25152395 source Swiss-Prot : SWS_FT_FI1

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