eF-site ID 2nu9-B PDB Code 2nu9 Chain B 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 B:  MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGA GPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRR VVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINP LVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHG GEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKK LADSGLNIIAAKGLTDAAQQVVAAV Description Functional site 1) chain B residue 53 type sequence G description BINDING SITE FOR RESIDUE SO4 B 389 source : AC1 2) chain B residue 54 type sequence R description BINDING SITE FOR RESIDUE SO4 B 389 source : AC1 3) chain B residue 55 type sequence G description BINDING SITE FOR RESIDUE SO4 B 389 source : AC1 4) chain B residue 213 type sequence D description BINDING SITE FOR RESIDUE SO4 B 389 source : AC1 5) chain B residue 1 type sequence M description BINDING SITE FOR RESIDUE SO4 B 390 source : AC2 6) chain B residue 220 type sequence G description BINDING SITE FOR RESIDUE SO4 B 390 source : AC2 7) chain B residue 233 type sequence R description BINDING SITE FOR RESIDUE SO4 B 390 source : AC2 8) chain B residue 33 type sequence E description BINDING SITE FOR RESIDUE COA D 301 source : BC1 9) chain B residue 36 type sequence S description BINDING SITE FOR RESIDUE COA D 301 source : BC1 10) chain B residue 66 type sequence K description BINDING SITE FOR RESIDUE COA D 301 source : BC1 11) chain B residue 161 type sequence R description BINDING SITE FOR RESIDUE COA F 400 source : BC2 12) chain B residue 109 type catalytic sequence Y description 476 source MCSA : MCSA1 13) chain B residue 197 type catalytic sequence E description 476 source MCSA : MCSA1 14) 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 15) 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 16) 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 17) 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 18) 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 19) 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 20) 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 21) chain B residue 264 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00558 source Swiss-Prot : SWS_FT_FI2 22) chain B residue 321 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00558 source Swiss-Prot : SWS_FT_FI2 23) 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

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