eF-site ID 1scu-ABDE PDB Code 1scu Chain A, B, D, E click to enlarge Title THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA COLI AT 2.5 ANGSTROMS RESOLUTION Classification LIGASE (ATP-BINDING) Compound SUCCINYL-COA SYNTHETASE, ALPHA SUBUNIT Source (SUCC_ECOLI) Sequence A:  SILIDKNTKVICQGFTGSQGTFHSEQAIAYGTKMVGGVTP GKGGTTHLGLPVFNTVREAVAATGATASVIYVPAPFCKDS ILEAIDAGIKLIITITEGIPTLDMLTVKVKLDEAGVRMIG PNCPGVITPGECKIGIQPGHIHKPGKVGIVSRSGTLTYEA VKQTTDYGFGQSTCVGIGGDPIPGSNFIDILEMFEKDPQT EAIVMIGEIGGSAEEEAAAYIKEHVTKPVVGYIAGVTAPK GKRMGXAGAIIAGGKGTADEKFAALEAAGVKTVRSLADIG EALKTVLK B:  MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGA GPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRR VVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINP LVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHG GEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKK LADSGLNIIAAKGLTDAAQQVVAAVEGK D:  SILIDKNTKVICQGFTGSQGTFHSEQAIAYGTKMVGGVTP GKGGTTHLGLPVFNTVREAVAATGATASVIYVPAPFCKDS ILEAIDAGIKLIITITEGIPTLDMLTVKVKLDEAGVRMIG PNCPGVITPGECKIGIQPGHIHKPGKVGIVSRSGTLTYEA VKQTTDYGFGQSTCVGIGGDPIPGSNFIDILEMFEKDPQT EAIVMIGEIGGSAEEEAAAYIKEHVTKPVVGYIAGVTAPK GKRMGXAGAIIAGGKGTADEKFAALEAAGVKTVRSLADIG EALKTVLK E:  MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGA GPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRR VVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINP LVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHG GEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKK LADSGLNIIAAKGLTDAAQQVVAAVEGK Description (1)  SUCCINYL-COA SYNTHETASE (SUCCINATE-COA LIGASE) (ADP-FORMING) (E.C.6.2.1.5) Functional site 1) chain A residue 14 type sequence G description BINDING SITE FOR RESIDUE COA A 289 source : AC1 2) chain A residue 16 type sequence T description BINDING SITE FOR RESIDUE COA A 289 source : AC1 3) chain A residue 17 type sequence G description BINDING SITE FOR RESIDUE COA A 289 source : AC1 4) chain A residue 18 type sequence S description BINDING SITE FOR RESIDUE COA A 289 source : AC1 5) chain A residue 19 type sequence Q description BINDING SITE FOR RESIDUE COA A 289 source : AC1 6) chain A residue 38 type sequence V description BINDING SITE FOR RESIDUE COA A 289 source : AC1 7) chain A residue 39 type sequence T description BINDING SITE FOR RESIDUE COA A 289 source : AC1 8) chain A residue 40 type sequence P description BINDING SITE FOR RESIDUE COA A 289 source : AC1 9) chain A residue 42 type sequence K description BINDING SITE FOR RESIDUE COA A 289 source : AC1 10) chain A residue 71 type sequence Y description BINDING SITE FOR RESIDUE COA A 289 source : AC1 11) chain A residue 72 type sequence V description BINDING SITE FOR RESIDUE COA A 289 source : AC1 12) chain A residue 73 type sequence P description BINDING SITE FOR RESIDUE COA A 289 source : AC1 13) chain A residue 80 type sequence S description BINDING SITE FOR RESIDUE COA A 289 source : AC1 14) chain A residue 95 type sequence I description BINDING SITE FOR RESIDUE COA A 289 source : AC1 15) chain A residue 96 type sequence T description BINDING SITE FOR RESIDUE COA A 289 source : AC1 16) chain A residue 97 type sequence E description BINDING SITE FOR RESIDUE COA A 289 source : AC1 17) chain A residue 122 type sequence N description BINDING SITE FOR RESIDUE COA A 289 source : AC1 18) chain A residue 123 type sequence C description BINDING SITE FOR RESIDUE COA A 289 source : AC1 19) chain A residue 124 type sequence P description BINDING SITE FOR RESIDUE COA A 289 source : AC1 20) chain B residue 161 type sequence R description BINDING SITE FOR RESIDUE COA A 289 source : AC1 21) chain E residue 29 type sequence R description BINDING SITE FOR RESIDUE COA A 289 source : AC1 22) chain E residue 33 type sequence E description BINDING SITE FOR RESIDUE COA A 289 source : AC1 23) chain E residue 36 type sequence S description BINDING SITE FOR RESIDUE COA A 289 source : AC1 24) chain E residue 66 type sequence K description BINDING SITE FOR RESIDUE COA A 289 source : AC1 25) chain B residue 33 type sequence E description BINDING SITE FOR RESIDUE COA D 289 source : AC2 26) chain B residue 36 type sequence S description BINDING SITE FOR RESIDUE COA D 289 source : AC2 27) chain B residue 66 type sequence K description BINDING SITE FOR RESIDUE COA D 289 source : AC2 28) chain D residue 14 type sequence G description BINDING SITE FOR RESIDUE COA D 289 source : AC2 29) chain D residue 16 type sequence T description BINDING SITE FOR RESIDUE COA D 289 source : AC2 30) chain D residue 17 type sequence G description BINDING SITE FOR RESIDUE COA D 289 source : AC2 31) chain D residue 18 type sequence S description BINDING SITE FOR RESIDUE COA D 289 source : AC2 32) chain D residue 19 type sequence Q description BINDING SITE FOR RESIDUE COA D 289 source : AC2 33) chain D residue 38 type sequence V description BINDING SITE FOR RESIDUE COA D 289 source : AC2 34) chain D residue 40 type sequence P description BINDING SITE FOR RESIDUE COA D 289 source : AC2 35) chain D residue 42 type sequence K description BINDING SITE FOR RESIDUE COA D 289 source : AC2 36) chain D residue 71 type sequence Y description BINDING SITE FOR RESIDUE COA D 289 source : AC2 37) chain D residue 72 type sequence V description BINDING SITE FOR RESIDUE COA D 289 source : AC2 38) chain D residue 73 type sequence P description BINDING SITE FOR RESIDUE COA D 289 source : AC2 39) chain D residue 80 type sequence S description BINDING SITE FOR RESIDUE COA D 289 source : AC2 40) chain D residue 95 type sequence I description BINDING SITE FOR RESIDUE COA D 289 source : AC2 41) chain D residue 96 type sequence T description BINDING SITE FOR RESIDUE COA D 289 source : AC2 42) chain D residue 97 type sequence E description BINDING SITE FOR RESIDUE COA D 289 source : AC2 43) chain D residue 122 type sequence N description BINDING SITE FOR RESIDUE COA D 289 source : AC2 44) chain D residue 123 type sequence C description BINDING SITE FOR RESIDUE COA D 289 source : AC2 45) chain B residue 109 type catalytic sequence Y description 476 source MCSA : MCSA1 46) chain B residue 197 type catalytic sequence E description 476 source MCSA : MCSA1 47) chain E residue 109 type catalytic sequence Y description 476 source MCSA : MCSA2 48) chain E residue 197 type catalytic sequence E description 476 source MCSA : MCSA2 49) chain A residue 159 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01988 source Swiss-Prot : SWS_FT_FI3 50) chain D residue 159 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01988 source Swiss-Prot : SWS_FT_FI3 51) chain B residue 257-282 type prosite sequence GNIGCMVNGAGLAMGTMDIVKLHGGE description SUCCINYL_COA_LIG_3 ATP-citrate lyase / succinyl-CoA ligases family signature 3. GnIgcMvNGAGLAmgtmDiVklhgGE source prosite : PS01217 52) chain A residue 235-248 type prosite sequence GVTAPKGKRMGXAG description SUCCINYL_COA_LIG_2 ATP-citrate lyase / succinyl-CoA ligases family active site. GvtApkgk...RMGHAG source prosite : PS00399 53) chain A residue 151-180 type prosite sequence SRSGTLTYEAVKQTTDYGFGQSTCVGIGGD description SUCCINYL_COA_LIG_1 ATP-citrate lyase / succinyl-CoA ligases family signature 1. SRSGTLTyEavkqttdygfGqstcVGIGGD source prosite : PS01216 54) chain B residue 46 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 55) chain E residue 99 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 56) chain E residue 102 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 57) chain E residue 107 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 58) chain E residue 199 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 59) chain E residue 213 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 60) chain B residue 53 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 61) chain B residue 99 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 62) chain B residue 102 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 63) chain B residue 107 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 64) chain B residue 199 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 65) chain B residue 213 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 66) chain E residue 46 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 67) chain E residue 53 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 68) chain B residue 264 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00558 source Swiss-Prot : SWS_FT_FI2 69) chain B residue 321 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00558 source Swiss-Prot : SWS_FT_FI2 70) chain E residue 264 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00558 source Swiss-Prot : SWS_FT_FI2 71) chain E residue 321 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00558 source Swiss-Prot : SWS_FT_FI2 72) chain D residue 43 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00558 source Swiss-Prot : SWS_FT_FI2 73) chain D residue 96 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00558 source Swiss-Prot : SWS_FT_FI2

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