eF-site ID 2fp4-B PDB Code 2fp4 Chain B click to enlarge Title Crystal structure of pig GTP-specific succinyl-CoA synthetase in complex with GTP Classification LIGASE Compound Succinyl-CoA ligase [GDP-forming] alpha-chain, mitochondrial Source Sus scrofa (Pig) (SUCB2_PIG) Sequence B:  MNLQEYQSKKLMSDNGVKVQRFFVADTANEALEAAKRLNA KEIVLKAQILAGGRGKGVFSSGLKGGVHLTKDPEVVGQLA KQMIGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAIL MDRSCNGPVLVGSPQGGVDIEEVAASNPELIFKEQIDIIE GIKDSQAQRMAENLGFLGPLQNQAADQIKKLYNLFLKIDA TQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMD DKSENEPIENEAAKYDLKYIGLDGNIACFVNGAGLAMATC DIIFLNGGKPANFLDLGGGVKESQVYQAFKLLTADPKVEA ILVNIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTN VHEAQNILTNSGLPITSAVDLEDAAKKAVASVT Description (1)  Succinyl-CoA ligase [GDP-forming] alpha-chain, mitochondrial (E.C.6.2.1.4), Succinyl-CoA ligase [GDP-forming] beta-chain, mitochondrial precursor (E.C.6.2.1.4) Functional site 1) chain B residue 206 type sequence N description BINDING SITE FOR RESIDUE K B 401 source : AC1 2) chain B residue 220 type sequence D description BINDING SITE FOR RESIDUE K B 401 source : AC1 3) chain B residue 165 type sequence S description BINDING SITE FOR RESIDUE MG B 402 source : AC2 4) chain B residue 20 type sequence Q description BINDING SITE FOR RESIDUE GTP B 403 source : AC3 5) chain B residue 44 type sequence V description BINDING SITE FOR RESIDUE GTP B 403 source : AC3 6) chain B residue 52 type sequence G description BINDING SITE FOR RESIDUE GTP B 403 source : AC3 7) chain B residue 53 type sequence G description BINDING SITE FOR RESIDUE GTP B 403 source : AC3 8) chain B residue 54 type sequence R description BINDING SITE FOR RESIDUE GTP B 403 source : AC3 9) chain B residue 55 type sequence G description BINDING SITE FOR RESIDUE GTP B 403 source : AC3 10) chain B residue 67 type sequence V description BINDING SITE FOR RESIDUE GTP B 403 source : AC3 11) chain B residue 69 type sequence L description BINDING SITE FOR RESIDUE GTP B 403 source : AC3 12) chain B residue 108 type sequence A description BINDING SITE FOR RESIDUE GTP B 403 source : AC3 13) chain B residue 109 type sequence L description BINDING SITE FOR RESIDUE GTP B 403 source : AC3 14) chain B residue 114 type sequence E description BINDING SITE FOR RESIDUE GTP B 403 source : AC3 15) chain B residue 219 type sequence F description BINDING SITE FOR RESIDUE GTP B 403 source : AC3 16) chain B residue 220 type sequence D description BINDING SITE FOR RESIDUE GTP B 403 source : AC3 17) chain B residue 222 type sequence K description BINDING SITE FOR RESIDUE GTP B 403 source : AC3 18) chain B residue 55 type sequence G description BINDING SITE FOR RESIDUE GTP B 404 source : AC4 19) chain B residue 56 type sequence K description BINDING SITE FOR RESIDUE GTP B 404 source : AC4 20) chain B residue 64 type sequence K description BINDING SITE FOR RESIDUE GTP B 404 source : AC4 21) chain B residue 163 type sequence K description BINDING SITE FOR RESIDUE GTP B 404 source : AC4 22) chain B residue 164 type sequence D description BINDING SITE FOR RESIDUE GTP B 404 source : AC4 23) chain B residue 165 type sequence S description BINDING SITE FOR RESIDUE GTP B 404 source : AC4 24) chain B residue 168 type sequence Q description BINDING SITE FOR RESIDUE GTP B 404 source : AC4 25) chain B residue 169 type sequence R description BINDING SITE FOR RESIDUE GTP B 404 source : AC4 26) chain B residue 172 type sequence E description BINDING SITE FOR RESIDUE GTP B 404 source : AC4 27) chain B residue 53 type ACT_SITE sequence G description Tele-phosphohistidine intermediate => ECO:0000255|HAMAP-Rule:MF_03222, ECO:0000269|PubMed:10873456, ECO:0000269|PubMed:16481318 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 109 type ACT_SITE sequence L description Tele-phosphohistidine intermediate => ECO:0000255|HAMAP-Rule:MF_03222, ECO:0000269|PubMed:10873456, ECO:0000269|PubMed:16481318 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 190 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q96I99 source Swiss-Prot : SWS_FT_FI8 30) chain B residue 254 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q96I99 source Swiss-Prot : SWS_FT_FI8 31) chain B residue 102 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WUM5 source Swiss-Prot : SWS_FT_FI5 32) chain B residue 163 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WUM5 source Swiss-Prot : SWS_FT_FI5 33) chain B residue 234 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WUM5 source Swiss-Prot : SWS_FT_FI5 34) chain B residue 310 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WUM5 source Swiss-Prot : SWS_FT_FI5 35) chain B residue 349 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WUM5 source Swiss-Prot : SWS_FT_FI5 36) chain B residue 386 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WUM5 source Swiss-Prot : SWS_FT_FI5 37) chain B residue 301 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q9WUM5 source Swiss-Prot : SWS_FT_FI6 38) chain B residue 264-289 type prosite sequence GNIACFVNGAGLAMATCDIIFLNGGK description SUCCINYL_COA_LIG_3 ATP-citrate lyase / succinyl-CoA ligases family signature 3. GnIacFvNGAGLAmatcDiIflngGK source prosite : PS01217 39) chain B residue 328 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03222, ECO:0000269|PubMed:27487822 source Swiss-Prot : SWS_FT_FI3 40) chain B residue 110 type MOD_RES sequence D description N6-acetyllysine => ECO:0000250|UniProtKB:P53597 source Swiss-Prot : SWS_FT_FI4

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