eF-site ID 1kf0-A PDB Code 1kf0 Chain A click to enlarge Title Crystal Structure of Pig Muscle Phosphoglycerate Kinase Ternary Complex with AMP-PCP and 3PG Classification TRANSFERASE Compound Phosphoglycerate Kinase Source ORGANISM_COMMON: pig; ORGANISM_SCIENTIFIC: Sus scrofa; Sequence A:  SLSNKLTLDKLNVKGKRVVMRVDFNVPMKNNQITNNQRIK AAVPSIKFCLDDGAKSVVLMSHLGRPDGSPMPDKYSLQPV AVELKSLLGKDVLFLKDCVGPEVEKACADPAAGSVILLEN LRFHVEEEGKGKDASGNKVKAEPAKIKTFRASLSKLGDVY VNDAFGTAHRAHSSMVGVNLPKKAGGFLMKKELNYFAKAL ESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGMA FTFLKVLNNMEIGTSLFDEEGAKIVKNLMSKAEKNGVKIT LPVDFVTADKFDEHAKTGQATVASGIPAGWMGLDCGPESS KKYSEAVARAKQIVWNGPVGVFEWEAFAQGTKALMDEVVK ATSRGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASLE LLEGKVLPGVDALSNV Description Functional site 1) chain A residue 218 type sequence D description BINDING SITE FOR RESIDUE MG A 518 source : AC1 2) chain A residue 23 type sequence D description BINDING SITE FOR RESIDUE 3PG A 417 source : AC2 3) chain A residue 25 type sequence N description BINDING SITE FOR RESIDUE 3PG A 417 source : AC2 4) chain A residue 38 type sequence R description BINDING SITE FOR RESIDUE 3PG A 417 source : AC2 5) chain A residue 62 type sequence H description BINDING SITE FOR RESIDUE 3PG A 417 source : AC2 6) chain A residue 65 type sequence R description BINDING SITE FOR RESIDUE 3PG A 417 source : AC2 7) chain A residue 122 type sequence R description BINDING SITE FOR RESIDUE 3PG A 417 source : AC2 8) chain A residue 166 type sequence G description BINDING SITE FOR RESIDUE 3PG A 417 source : AC2 9) chain A residue 170 type sequence R description BINDING SITE FOR RESIDUE 3PG A 417 source : AC2 10) chain A residue 213 type sequence G description BINDING SITE FOR RESIDUE ACP A 418 source : AC3 11) chain A residue 214 type sequence A description BINDING SITE FOR RESIDUE ACP A 418 source : AC3 12) chain A residue 215 type sequence K description BINDING SITE FOR RESIDUE ACP A 418 source : AC3 13) chain A residue 219 type sequence K description BINDING SITE FOR RESIDUE ACP A 418 source : AC3 14) chain A residue 237 type sequence G description BINDING SITE FOR RESIDUE ACP A 418 source : AC3 15) chain A residue 238 type sequence G description BINDING SITE FOR RESIDUE ACP A 418 source : AC3 16) chain A residue 241 type sequence F description BINDING SITE FOR RESIDUE ACP A 418 source : AC3 17) chain A residue 312 type sequence G description BINDING SITE FOR RESIDUE ACP A 418 source : AC3 18) chain A residue 340 type sequence G description BINDING SITE FOR RESIDUE ACP A 418 source : AC3 19) chain A residue 341 type sequence V description BINDING SITE FOR RESIDUE ACP A 418 source : AC3 20) chain A residue 343 type sequence E description BINDING SITE FOR RESIDUE ACP A 418 source : AC3 21) chain A residue 374 type sequence D description BINDING SITE FOR RESIDUE ACP A 418 source : AC3 22) chain A residue 17-27 type prosite sequence RVVMRVDFNVP description PGLYCERATE_KINASE Phosphoglycerate kinase signature. RVVMRvDfNVP source prosite : PS00111 23) chain A residue 24 type BINDING sequence F description BINDING => ECO:0000269|PubMed:11178909 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 39 type BINDING sequence I description BINDING => ECO:0000269|PubMed:11178909 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 63 type BINDING sequence L description BINDING => ECO:0000269|PubMed:11178909 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 123 type BINDING sequence F description BINDING => ECO:0000269|PubMed:11178909 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 171 type BINDING sequence A description BINDING => ECO:0000269|PubMed:11178909 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 131 type MOD_RES sequence G description N6-malonyllysine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI10 29) chain A residue 196 type MOD_RES sequence F description Phosphotyrosine => ECO:0000250|UniProtKB:P00558 source Swiss-Prot : SWS_FT_FI11 30) chain A residue 216 type MOD_RES sequence V description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P00558 source Swiss-Prot : SWS_FT_FI12 31) chain A residue 220 type MOD_RES sequence I description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P00558 source Swiss-Prot : SWS_FT_FI12 32) chain A residue 323 type MOD_RES sequence Y description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P00558 source Swiss-Prot : SWS_FT_FI12 33) chain A residue 220 type BINDING sequence I description BINDING => ECO:0000269|PubMed:15035615 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 313 type BINDING sequence L description BINDING => ECO:0000269|PubMed:15035615 source Swiss-Prot : SWS_FT_FI2 35) chain A residue 344 type BINDING sequence W description BINDING => ECO:0000269|PubMed:15035615 source Swiss-Prot : SWS_FT_FI2 36) chain A residue 373 type BINDING sequence G description BINDING => ECO:0000269|PubMed:15035615 source Swiss-Prot : SWS_FT_FI2 37) chain A residue 2 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:P00558 source Swiss-Prot : SWS_FT_FI3 38) chain A residue 4 type MOD_RES sequence N description Phosphoserine => ECO:0000250|UniProtKB:P00558 source Swiss-Prot : SWS_FT_FI3 39) chain A residue 203 type MOD_RES sequence P description Phosphoserine => ECO:0000250|UniProtKB:P00558 source Swiss-Prot : SWS_FT_FI3 40) chain A residue 6 type MOD_RES sequence L description N6-succinyllysine => ECO:0000250|UniProtKB:P09411 source Swiss-Prot : SWS_FT_FI4 41) chain A residue 191 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P09411 source Swiss-Prot : SWS_FT_FI4 42) chain A residue 11 type MOD_RES sequence L description N6-acetyllysine => ECO:0000250|UniProtKB:P00558 source Swiss-Prot : SWS_FT_FI5 43) chain A residue 75 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P00558 source Swiss-Prot : SWS_FT_FI5 44) chain A residue 86 type MOD_RES sequence S description N6-acetyllysine => ECO:0000250|UniProtKB:P00558 source Swiss-Prot : SWS_FT_FI5 45) chain A residue 146 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P00558 source Swiss-Prot : SWS_FT_FI5 46) chain A residue 199 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:P00558 source Swiss-Prot : SWS_FT_FI5 47) chain A residue 267 type MOD_RES sequence N description N6-acetyllysine => ECO:0000250|UniProtKB:P00558 source Swiss-Prot : SWS_FT_FI5 48) chain A residue 291 type MOD_RES sequence F description N6-acetyllysine => ECO:0000250|UniProtKB:P00558 source Swiss-Prot : SWS_FT_FI5 49) chain A residue 48 type MOD_RES sequence F description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09411 source Swiss-Prot : SWS_FT_FI6 50) chain A residue 76 type MOD_RES sequence S description Phosphotyrosine => ECO:0000250|UniProtKB:P09411 source Swiss-Prot : SWS_FT_FI7 51) chain A residue 91 type MOD_RES sequence D description N6-acetyllysine => ECO:0000250|UniProtKB:P09411 source Swiss-Prot : SWS_FT_FI8 52) chain A residue 361 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:P09411 source Swiss-Prot : SWS_FT_FI8 53) chain A residue 97 type MOD_RES sequence D description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P00558 source Swiss-Prot : SWS_FT_FI9

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