eF-site ID 1scu-B PDB Code 1scu Chain B 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 B:  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 B residue 161 type sequence R description BINDING SITE FOR RESIDUE COA A 289 source : AC1 2) chain B residue 33 type sequence E description BINDING SITE FOR RESIDUE COA D 289 source : AC2 3) chain B residue 36 type sequence S description BINDING SITE FOR RESIDUE COA D 289 source : AC2 4) chain B residue 66 type sequence K description BINDING SITE FOR RESIDUE COA D 289 source : AC2 5) chain B residue 109 type catalytic sequence Y description 476 source MCSA : MCSA1 6) chain B residue 197 type catalytic sequence E description 476 source MCSA : MCSA1 7) 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 8) 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 9) 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 10) 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 11) 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 12) 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 13) 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 14) 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 15) chain B residue 264 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00558 source Swiss-Prot : SWS_FT_FI2 16) 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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