eF-site ID 1cqi-B PDB Code 1cqi Chain B click to enlarge Title Crystal Structure of the Complex of ADP and MG2+ with Dephosphorylated E. Coli Succinyl-CoA Synthetase Classification LIGASE Compound PROTEIN (SUCCINYL-COA SYNTHETASE ALPHA CHAIN) Source (SUCC_ECOLI) Sequence B:  MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGA GPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRR VVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINP LVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHG GEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKK LADSGLNIIAAKGLTDAAQQVVAAV Description (1)  SUCCINYL-COA SYNTHETASE ALPHA AND BETA SUBUNITS (E.C.6.2.1.5) Functional site 1) chain B residue 199 type sequence N description BINDING SITE FOR RESIDUE MG B 501 source : AC1 2) chain B residue 213 type sequence D description BINDING SITE FOR RESIDUE MG B 501 source : AC1 3) chain B residue 265 type sequence G description BINDING SITE FOR RESIDUE PO4 A 601 source : AC3 4) chain B residue 266 type sequence A description BINDING SITE FOR RESIDUE PO4 A 601 source : AC3 5) chain B residue 267 type sequence G description BINDING SITE FOR RESIDUE PO4 A 601 source : AC3 6) chain B residue 161 type sequence R description BINDING SITE FOR RESIDUE COA A 701 source : AC5 7) chain B residue 29 type sequence R description BINDING SITE FOR RESIDUE COA D 702 source : AC6 8) chain B residue 33 type sequence E description BINDING SITE FOR RESIDUE COA D 702 source : AC6 9) chain B residue 36 type sequence S description BINDING SITE FOR RESIDUE COA D 702 source : AC6 10) chain B residue 66 type sequence K description BINDING SITE FOR RESIDUE COA D 702 source : AC6 11) chain B residue 44 type sequence V description BINDING SITE FOR RESIDUE ADP B 801 source : AC7 12) chain B residue 46 type sequence K description BINDING SITE FOR RESIDUE ADP B 801 source : AC7 13) chain B residue 53 type sequence G description BINDING SITE FOR RESIDUE ADP B 801 source : AC7 14) chain B residue 54 type sequence R description BINDING SITE FOR RESIDUE ADP B 801 source : AC7 15) chain B residue 55 type sequence G description BINDING SITE FOR RESIDUE ADP B 801 source : AC7 16) chain B residue 99 type sequence E description BINDING SITE FOR RESIDUE ADP B 801 source : AC7 17) chain B residue 100 type sequence A description BINDING SITE FOR RESIDUE ADP B 801 source : AC7 18) chain B residue 101 type sequence A description BINDING SITE FOR RESIDUE ADP B 801 source : AC7 19) chain B residue 102 type sequence T description BINDING SITE FOR RESIDUE ADP B 801 source : AC7 20) chain B residue 107 type sequence E description BINDING SITE FOR RESIDUE ADP B 801 source : AC7 21) chain B residue 199 type sequence N description BINDING SITE FOR RESIDUE ADP B 801 source : AC7 22) chain B residue 200 type sequence P description BINDING SITE FOR RESIDUE ADP B 801 source : AC7 23) chain B residue 212 type sequence L description BINDING SITE FOR RESIDUE ADP B 801 source : AC7 24) chain B residue 213 type sequence D description BINDING SITE FOR RESIDUE ADP B 801 source : AC7 25) chain B residue 109 type catalytic sequence Y description 476 source MCSA : MCSA1 26) chain B residue 197 type catalytic sequence E description 476 source MCSA : MCSA1 27) 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 28) 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 29) 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 30) 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 31) 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 32) 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 33) 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 34) 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 35) chain B residue 264 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00558 source Swiss-Prot : SWS_FT_FI2 36) chain B residue 321 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00558 source Swiss-Prot : SWS_FT_FI2

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