eF-site ID 2nu9-I PDB Code 2nu9 Chain I 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 I:  MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGA GPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRR VVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINP LVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHG GEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKK LADSGLNIIAAKGLTDAAQQVVAAV Description Functional site 1) chain I residue 52 type sequence G description BINDING SITE FOR RESIDUE SO4 I 389 source : AC7 2) chain I residue 53 type sequence G description BINDING SITE FOR RESIDUE SO4 I 389 source : AC7 3) chain I residue 54 type sequence R description BINDING SITE FOR RESIDUE SO4 I 389 source : AC7 4) chain I residue 55 type sequence G description BINDING SITE FOR RESIDUE SO4 I 389 source : AC7 5) chain I residue 213 type sequence D description BINDING SITE FOR RESIDUE SO4 I 389 source : AC7 6) chain I residue 1 type sequence M description BINDING SITE FOR RESIDUE SO4 I 390 source : AC8 7) chain I residue 220 type sequence G description BINDING SITE FOR RESIDUE SO4 I 390 source : AC8 8) chain I residue 233 type sequence R description BINDING SITE FOR RESIDUE SO4 I 390 source : AC8 9) chain I residue 161 type sequence R description BINDING SITE FOR RESIDUE COA D 301 source : BC1 10) chain I residue 29 type sequence R description BINDING SITE FOR RESIDUE COA F 400 source : BC2 11) chain I residue 33 type sequence E description BINDING SITE FOR RESIDUE COA F 400 source : BC2 12) chain I residue 36 type sequence S description BINDING SITE FOR RESIDUE COA F 400 source : BC2 13) chain I residue 66 type sequence K description BINDING SITE FOR RESIDUE COA F 400 source : BC2 14) chain I residue 109 type catalytic sequence Y description 476 source MCSA : MCSA4 15) chain I residue 197 type catalytic sequence E description 476 source MCSA : MCSA4 16) chain I residue 46 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 17) chain I residue 53 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 18) chain I residue 99 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 19) chain I residue 102 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 20) chain I residue 107 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 21) chain I residue 199 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 22) chain I residue 213 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 source Swiss-Prot : SWS_FT_FI1 23) chain I residue 264 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00558 source Swiss-Prot : SWS_FT_FI2 24) chain I residue 321 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00558 source Swiss-Prot : SWS_FT_FI2

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