eF-site ID 1k3d-A PDB Code 1k3d Chain A click to enlarge Title Phosphoenolpyruvate carboxykinase in complex with ADP and AlF3 Classification LYASE Compound Phosphoenolpyruvate carboxykinase Source null (PPCK_ECOLI) Sequence A:  GLTPQELEAYGISDVHDIVYNPSYDLLYQEELDPSLTGYE RGVLTNLGAVAVDTGIFTGRSPKDKYIVRDDTTRDTFWWA DKGKGKNDNKPLSPETWQHLKGLVTRQLSGKRLFVVDAFC GANPDTRLSVRFITEVAWQAHFVKNMFIRPSDEELAGFKP DFIVMNGAKCTNPQWKEQGLNSENFVAFNLTERMQLIGGT WYGGEMKKGMFSMMNYLLPLKGIASMHCSANVGEKGDVAV FFGLSGTGKTTLSTDPKRRLIGDDEHGWDDDGVFNFEGGC YAKTIKLSKEAEPEIYNAIRRDALLENVTVREDGTIDFDD GSKTENTRVSYPIYHIDNIVKPVSKAGHATKVIFLTADAF GVLPPVSRLTADQTQYHFLSGFTAKLAGTERGITEPTPTF SACFGAAFLSLHPTQYAEVLVKRMQAAGAQAYLVNTGWNG TGKRISIKDTRAIIDAILNGSLDNAETFTLPMFNLAIPTE LPGVDTKILDPRNTYASPEQWQEKAETLAKLFIDNFDKYT DTPAGAALVAAGPKL Description Functional site 1) chain A residue 255 type sequence T description BINDING SITE FOR RESIDUE MG A 998 source : AC1 2) chain A residue 268 type sequence D description BINDING SITE FOR RESIDUE MG A 998 source : AC1 3) chain A residue 249 type sequence L description BINDING SITE FOR RESIDUE ADP A 541 source : AC2 4) chain A residue 250 type sequence S description BINDING SITE FOR RESIDUE ADP A 541 source : AC2 5) chain A residue 251 type sequence G description BINDING SITE FOR RESIDUE ADP A 541 source : AC2 6) chain A residue 252 type sequence T description BINDING SITE FOR RESIDUE ADP A 541 source : AC2 7) chain A residue 253 type sequence G description BINDING SITE FOR RESIDUE ADP A 541 source : AC2 8) chain A residue 254 type sequence K description BINDING SITE FOR RESIDUE ADP A 541 source : AC2 9) chain A residue 255 type sequence T description BINDING SITE FOR RESIDUE ADP A 541 source : AC2 10) chain A residue 256 type sequence T description BINDING SITE FOR RESIDUE ADP A 541 source : AC2 11) chain A residue 288 type sequence K description BINDING SITE FOR RESIDUE ADP A 541 source : AC2 12) chain A residue 297 type sequence E description BINDING SITE FOR RESIDUE ADP A 541 source : AC2 13) chain A residue 441 type sequence T description BINDING SITE FOR RESIDUE ADP A 541 source : AC2 14) chain A residue 449 type sequence R description BINDING SITE FOR RESIDUE ADP A 541 source : AC2 15) chain A residue 450 type sequence I description BINDING SITE FOR RESIDUE ADP A 541 source : AC2 16) chain A residue 451 type sequence S description BINDING SITE FOR RESIDUE ADP A 541 source : AC2 17) chain A residue 452 type sequence I description BINDING SITE FOR RESIDUE ADP A 541 source : AC2 18) chain A residue 455 type sequence T description BINDING SITE FOR RESIDUE ADP A 541 source : AC2 19) chain A residue 213 type sequence K description BINDING SITE FOR RESIDUE AF3 A 999 source : AC3 20) chain A residue 232 type sequence H description BINDING SITE FOR RESIDUE AF3 A 999 source : AC3 21) chain A residue 250 type sequence S description BINDING SITE FOR RESIDUE AF3 A 999 source : AC3 22) chain A residue 269 type sequence D description BINDING SITE FOR RESIDUE AF3 A 999 source : AC3 23) chain A residue 333 type sequence R description BINDING SITE FOR RESIDUE AF3 A 999 source : AC3 24) chain A residue 65 type catalytic sequence R description 51 source MCSA : MCSA1 25) chain A residue 213 type catalytic sequence K description 51 source MCSA : MCSA1 26) chain A residue 232 type catalytic sequence H description 51 source MCSA : MCSA1 27) chain A residue 250 type catalytic sequence S description 51 source MCSA : MCSA1 28) chain A residue 254 type catalytic sequence K description 51 source MCSA : MCSA1 29) chain A residue 255 type catalytic sequence T description 51 source MCSA : MCSA1 30) chain A residue 269 type catalytic sequence D description 51 source MCSA : MCSA1 31) chain A residue 333 type catalytic sequence R description 51 source MCSA : MCSA1 32) 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 33) 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 34) 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 35) 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 36) chain A residue 149 type BINDING sequence K description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 37) chain A residue 150 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 38) chain A residue 152 type BINDING sequence F description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 283 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 40) 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 41) 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 42) 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 43) 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 44) 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 45) 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 46) 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 47) 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 48) chain A residue 265-280 type prosite sequence LIGDDEHGWDDDGVFN description PEPCK_ATP Phosphoenolpyruvate carboxykinase (ATP) signature. LIGDDEHgWdDdGVfN source prosite : PS00532

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