eF-site ID 2nu9-E PDB Code 2nu9 Chain E 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 E:  MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGA GPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRR VVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINP LVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHG GEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKK LADSGLNIIAAKGLTDAAQQVVAAV Description Functional site 1) chain E residue 52 type sequence G description BINDING SITE FOR RESIDUE SO4 E 389 source : AC3 2) chain E residue 53 type sequence G description BINDING SITE FOR RESIDUE SO4 E 389 source : AC3 3) chain E residue 54 type sequence R description BINDING SITE FOR RESIDUE SO4 E 389 source : AC3 4) chain E residue 55 type sequence G description BINDING SITE FOR RESIDUE SO4 E 389 source : AC3 5) chain E residue 213 type sequence D description BINDING SITE FOR RESIDUE SO4 E 389 source : AC3 6) chain E residue 1 type sequence M description BINDING SITE FOR RESIDUE SO4 E 390 source : AC4 7) chain E residue 220 type sequence G description BINDING SITE FOR RESIDUE SO4 E 390 source : AC4 8) chain E residue 233 type sequence R description BINDING SITE FOR RESIDUE SO4 E 390 source : AC4 9) chain E residue 33 type sequence E description BINDING SITE FOR RESIDUE COA A 300 source : AC9 10) chain E residue 36 type sequence S description BINDING SITE FOR RESIDUE COA A 300 source : AC9 11) chain E residue 66 type sequence K description BINDING SITE FOR RESIDUE COA A 300 source : AC9 12) chain E residue 109 type catalytic sequence Y description 476 source MCSA : MCSA2 13) chain E residue 197 type catalytic sequence E description 476 source MCSA : MCSA2 14) 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 15) 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 16) 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 17) 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 18) 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 19) 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 20) 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 21) chain E residue 264 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00558 source Swiss-Prot : SWS_FT_FI2 22) chain E residue 321 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00558 source Swiss-Prot : SWS_FT_FI2

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