eF-site ID 1aq2-A PDB Code 1aq2 Chain A click to enlarge Title PHOSPHOENOLPYRUVATE CARBOXYKINASE Classification KINASE Compound PHOSPHOENOLPYRUVATE CARBOXYKINASE Source null (PPCK_ECOLI) Sequence A:  NNGLTPQELEAYGISDVHDIVYNPSYDLLYQEELDPSLTG YERGVLTNLGAVAVDTGIFTGRSPKDKYIVRDDTTRDTFW WADKGKGKNDNKPLSPETWQHLKGLVTRQLSGKRLFVVDA FCGANPDTRLSVRFITEVAWQAHFVKNMFIRPSDEELAGF KPDFIVMNGAKCTNPQWKEQGLNSENFVAFNLTERMQLIG GTWYGGEMKKGMFSMMNYLLPLKGIASMHCSANVGEKGDV AVFFGLSGTGKTTLSTDPKRRLIGDDEHGWDDDGVFNFEG GCYAKTIKLSKEAEPEIYNAIRRDALLENVTVREDGTIDF DDGSKTENTRVSYPIYHIDNIVKPVSKAGHATKVIFLTAD AFGVLPPVSRLTADQTQYHFLSGFTAKLAGTITEPTPTFS ACFGAAFLSLHPTQYAEVLVKRMQAAGAQAYLVNTGWNGT GKRISIKDTRAIIDAILNGSLDNAETFTLPMFNLAIPTEL PGVDTKILDPRNTYASPEQWQEKAETLAKLFIDNFDKYTD TPAGAALVAAGPKL Description Functional site 1) chain A residue 65 type sequence R description ACTIVE SITE source : ACT 2) chain A residue 207 type sequence Y description ACTIVE SITE source : ACT 3) chain A residue 212 type sequence K description ACTIVE SITE source : ACT 4) chain A residue 213 type sequence K description ACTIVE SITE source : ACT 5) chain A residue 213 type sequence K description BINDING SITE FOR RESIDUE MN A 543 source : AC1 6) chain A residue 232 type sequence H description BINDING SITE FOR RESIDUE MN A 543 source : AC1 7) chain A residue 269 type sequence D description BINDING SITE FOR RESIDUE MN A 543 source : AC1 8) chain A residue 255 type sequence T description BINDING SITE FOR RESIDUE MG A 544 source : AC2 9) chain A residue 268 type sequence D description BINDING SITE FOR RESIDUE MG A 544 source : AC2 10) chain A residue 232 type sequence H description BINDING SITE FOR RESIDUE ATP A 541 source : AC3 11) chain A residue 249 type sequence L description BINDING SITE FOR RESIDUE ATP A 541 source : AC3 12) chain A residue 250 type sequence S description BINDING SITE FOR RESIDUE ATP A 541 source : AC3 13) chain A residue 251 type sequence G description BINDING SITE FOR RESIDUE ATP A 541 source : AC3 14) chain A residue 252 type sequence T description BINDING SITE FOR RESIDUE ATP A 541 source : AC3 15) chain A residue 253 type sequence G description BINDING SITE FOR RESIDUE ATP A 541 source : AC3 16) chain A residue 254 type sequence K description BINDING SITE FOR RESIDUE ATP A 541 source : AC3 17) chain A residue 255 type sequence T description BINDING SITE FOR RESIDUE ATP A 541 source : AC3 18) chain A residue 256 type sequence T description BINDING SITE FOR RESIDUE ATP A 541 source : AC3 19) chain A residue 269 type sequence D description BINDING SITE FOR RESIDUE ATP A 541 source : AC3 20) chain A residue 288 type sequence K description BINDING SITE FOR RESIDUE ATP A 541 source : AC3 21) chain A residue 290 type sequence I description BINDING SITE FOR RESIDUE ATP A 541 source : AC3 22) chain A residue 297 type sequence E description BINDING SITE FOR RESIDUE ATP A 541 source : AC3 23) chain A residue 333 type sequence R description BINDING SITE FOR RESIDUE ATP A 541 source : AC3 24) chain A residue 449 type sequence R description BINDING SITE FOR RESIDUE ATP A 541 source : AC3 25) chain A residue 450 type sequence I description BINDING SITE FOR RESIDUE ATP A 541 source : AC3 26) chain A residue 451 type sequence S description BINDING SITE FOR RESIDUE ATP A 541 source : AC3 27) chain A residue 452 type sequence I description BINDING SITE FOR RESIDUE ATP A 541 source : AC3 28) chain A residue 455 type sequence T description BINDING SITE FOR RESIDUE ATP A 541 source : AC3 29) chain A residue 65 type sequence R description BINDING SITE FOR RESIDUE PYR A 542 source : AC4 30) chain A residue 213 type sequence K description BINDING SITE FOR RESIDUE PYR A 542 source : AC4 31) chain A residue 286 type sequence Y description BINDING SITE FOR RESIDUE PYR A 542 source : AC4 32) chain A residue 333 type sequence R description BINDING SITE FOR RESIDUE PYR A 542 source : AC4 33) chain A residue 65 type catalytic sequence R description 51 source MCSA : MCSA1 34) chain A residue 213 type catalytic sequence K description 51 source MCSA : MCSA1 35) chain A residue 232 type catalytic sequence H description 51 source MCSA : MCSA1 36) chain A residue 250 type catalytic sequence S description 51 source MCSA : MCSA1 37) chain A residue 254 type catalytic sequence K description 51 source MCSA : MCSA1 38) chain A residue 255 type catalytic sequence T description 51 source MCSA : MCSA1 39) chain A residue 269 type catalytic sequence D description 51 source MCSA : MCSA1 40) chain A residue 333 type catalytic sequence R description 51 source MCSA : MCSA1 41) chain A residue 65 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:11724534 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 207 type BINDING sequence Y description BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:11724534 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 213 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:11724534 source Swiss-Prot : SWS_FT_FI1 44) chain A residue 333 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:11724534 source Swiss-Prot : SWS_FT_FI1 45) chain A residue 149 type BINDING sequence K description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 46) chain A residue 150 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 152 type BINDING sequence F description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 48) chain A residue 283 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 269 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|Ref.21 source Swiss-Prot : SWS_FT_FI3 50) chain A residue 232 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|Ref.21 source Swiss-Prot : SWS_FT_FI3 51) chain A residue 297 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:12837799, ECO:0000269|PubMed:17475535, ECO:0000269|PubMed:8599762, ECO:0000269|PubMed:9406547, ECO:0000269|Ref.20, ECO:0000269|Ref.21 source Swiss-Prot : SWS_FT_FI4 52) chain A residue 449 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:12837799, ECO:0000269|PubMed:17475535, ECO:0000269|PubMed:8599762, ECO:0000269|PubMed:9406547, ECO:0000269|Ref.20, ECO:0000269|Ref.21 source Swiss-Prot : SWS_FT_FI4 53) chain A residue 455 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:12837799, ECO:0000269|PubMed:17475535, ECO:0000269|PubMed:8599762, ECO:0000269|PubMed:9406547, ECO:0000269|Ref.20, ECO:0000269|Ref.21 source Swiss-Prot : SWS_FT_FI4 54) chain A residue 248 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:12837799, ECO:0000269|PubMed:17475535, ECO:0000269|PubMed:8599762, ECO:0000269|PubMed:9406547, ECO:0000269|Ref.20, ECO:0000269|Ref.21 source Swiss-Prot : SWS_FT_FI4 55) chain A residue 87 type MOD_RES sequence K description N6-acetyllysine => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI5 56) chain A residue 523 type MOD_RES sequence K description N6-acetyllysine => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI5 57) chain A residue 265-280 type prosite sequence LIGDDEHGWDDDGVFN description PEPCK_ATP Phosphoenolpyruvate carboxykinase (ATP) signature. LIGDDEHgWdDdGVfN source prosite : PS00532

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