eF-site ID 2nu9-G PDB Code 2nu9 Chain G click to enlarge Title C123aT Mutant of E. coli Succinyl-CoA Synthetase Orthorhombic Crystal Form Classification LIGASE Compound Succinyl-CoA ligase [ADP-forming] subunit alpha Source Escherichia coli (strain K12) (SUCC_ECOLI) Sequence G:  MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGA GPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRR VVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINP LVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHG GEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKK LADSGLNIIAAKGLTDAAQQVVAAV Description Functional site 1) chain G residue 52 type sequence G description BINDING SITE FOR RESIDUE SO4 G 389 source : AC5 2) chain G residue 53 type sequence G description BINDING SITE FOR RESIDUE SO4 G 389 source : AC5 3) chain G residue 54 type sequence R description BINDING SITE FOR RESIDUE SO4 G 389 source : AC5 4) chain G residue 55 type sequence G description BINDING SITE FOR RESIDUE SO4 G 389 source : AC5 5) chain G residue 213 type sequence D description BINDING SITE FOR RESIDUE SO4 G 389 source : AC5 6) chain G residue 1 type sequence M description BINDING SITE FOR RESIDUE SO4 G 390 source : AC6 7) chain G residue 220 type sequence G description BINDING SITE FOR RESIDUE SO4 G 390 source : AC6 8) chain G residue 233 type sequence R description BINDING SITE FOR RESIDUE SO4 G 390 source : AC6 9) chain G residue 29 type sequence R description BINDING SITE FOR RESIDUE COA H 401 source : BC3 10) chain G residue 33 type sequence E description BINDING SITE FOR RESIDUE COA H 401 source : BC3 11) chain G residue 36 type sequence S description BINDING SITE FOR RESIDUE COA H 401 source : BC3 12) chain G residue 66 type sequence K description BINDING SITE FOR RESIDUE COA H 401 source : BC3 13) chain G residue 109 type catalytic sequence Y description 476 source MCSA : MCSA3 14) chain G residue 197 type catalytic sequence E description 476 source MCSA : MCSA3 15) chain G residue 46 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 16) chain G residue 53 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 17) chain G residue 99 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 18) chain G residue 102 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 19) chain G residue 107 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 20) chain G residue 199 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 21) chain G residue 213 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 22) chain G residue 264 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00558 source Swiss-Prot : SWS_FT_FI2 23) chain G residue 321 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00558 source Swiss-Prot : SWS_FT_FI2

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