eF-site ID 1xkv-A PDB Code 1xkv Chain A click to enlarge Title Crystal Structure Of ATP-Dependent Phosphoenolpyruvate Carboxykinase From Thermus thermophilus HB8 Classification LYASE Compound ATP-dependent phosphoenolpyruvate carboxykinase Source null (Q5SLL5_THET8) Sequence A:  QRLEALGIHPKKRVFWNTVSPVLVEHTLLRGEGLLAHHGP LVVDTTPYTGRSPKDKFVVREPEVEGEIWWGEVNQPFAPE AFEALYQRVVQYLSERDLYVQDLYAGADRRYRLAVRVVTE SPWHALFARNMFILPRRFGAFVPGFTVVHAPYFQAVPERD GTRSEVFVGISFQRRLVLIVGTKYAGEIKKSIFTVMNYLM PKRGVFPMHASANVGKEGDVAVFFGLSGTGKTTLSTDPER PLIGDDEHGWSEDGVFNFEGGCYAKVIRLSPEHEPLIYKA SNQFEAILENVVVNPESRRVQWDDDSKTENTRSSYPIAHL ENVVESGVAGHPRAIFFLSADAYGVLPPIARLSPEEAMYY FLSGYTARVTEPRATFSACFGAPFLPMHPGVYARMLGEKI RKHAPRVYLVNTGWTGGPYGVGYRFPLPVTRALLKAALSG ALENVPYRRDPVFGFEVPLEAPGVPQELLNPRETWADKEA YDQQARKLARLFQENFQKYASGVAKEVAEAGPRTE Description Functional site 1) chain A residue 130 type sequence R description BINDING SITE FOR RESIDUE CA A 2001 source : AC1 2) chain A residue 131 type sequence N description BINDING SITE FOR RESIDUE CA A 2001 source : AC1 3) chain A residue 133 type sequence F description BINDING SITE FOR RESIDUE CA A 2001 source : AC1 4) chain A residue 267 type sequence G description BINDING SITE FOR RESIDUE CA A 2001 source : AC1 5) chain A residue 20 type sequence V description BINDING SITE FOR RESIDUE PO4 A 3001 source : AC3 6) chain A residue 21 type sequence S description BINDING SITE FOR RESIDUE PO4 A 3001 source : AC3 7) chain A residue 130 type sequence R description BINDING SITE FOR RESIDUE PO4 A 3001 source : AC3 8) chain A residue 137 type sequence R description BINDING SITE FOR RESIDUE PO4 A 3001 source : AC3 9) chain A residue 259 type sequence E description BINDING SITE FOR RESIDUE PO4 A 3002 source : AC4 10) chain A residue 413 type sequence K description BINDING SITE FOR RESIDUE PO4 A 3002 source : AC4 11) chain A residue 416 type sequence K description BINDING SITE FOR RESIDUE PO4 A 3002 source : AC4 12) chain A residue 417 type sequence H description BINDING SITE FOR RESIDUE PO4 A 3002 source : AC4 13) chain A residue 38 type sequence H description BINDING SITE FOR RESIDUE PO4 B 3003 source : AC5 14) chain A residue 233 type sequence L description BINDING SITE FOR RESIDUE ATP A 1001 source : AC9 15) chain A residue 234 type sequence S description BINDING SITE FOR RESIDUE ATP A 1001 source : AC9 16) chain A residue 235 type sequence G description BINDING SITE FOR RESIDUE ATP A 1001 source : AC9 17) chain A residue 236 type sequence T description BINDING SITE FOR RESIDUE ATP A 1001 source : AC9 18) chain A residue 237 type sequence G description BINDING SITE FOR RESIDUE ATP A 1001 source : AC9 19) chain A residue 238 type sequence K description BINDING SITE FOR RESIDUE ATP A 1001 source : AC9 20) chain A residue 239 type sequence T description BINDING SITE FOR RESIDUE ATP A 1001 source : AC9 21) chain A residue 240 type sequence T description BINDING SITE FOR RESIDUE ATP A 1001 source : AC9 22) chain A residue 272 type sequence K description BINDING SITE FOR RESIDUE ATP A 1001 source : AC9 23) chain A residue 426 type sequence T description BINDING SITE FOR RESIDUE ATP A 1001 source : AC9 24) chain A residue 438 type sequence R description BINDING SITE FOR RESIDUE ATP A 1001 source : AC9 25) chain A residue 439 type sequence F description BINDING SITE FOR RESIDUE ATP A 1001 source : AC9 26) chain A residue 444 type sequence T description BINDING SITE FOR RESIDUE ATP A 1001 source : AC9 27) chain A residue 66 type sequence E description BINDING SITE FOR RESIDUE GOL B 4002 source : BC2 28) chain A residue 67 type sequence G description BINDING SITE FOR RESIDUE GOL B 4002 source : BC2 29) chain A residue 71 type sequence W description BINDING SITE FOR RESIDUE GOL B 4002 source : BC2 30) chain A residue 52 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00453 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 191 type BINDING sequence Y description BINDING => ECO:0000255|HAMAP-Rule:MF_00453 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 197 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00453 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 253 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00453 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 281 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00453 source Swiss-Prot : SWS_FT_FI1 35) chain A residue 319 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00453 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 130 type BINDING sequence R description BINDING => ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1J3B, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9 source Swiss-Prot : SWS_FT_FI2 37) chain A residue 131 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1J3B, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9 source Swiss-Prot : SWS_FT_FI2 38) chain A residue 267 type BINDING sequence G description BINDING => ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1J3B, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 249-264 type prosite sequence LIGDDEHGWSEDGVFN description PEPCK_ATP Phosphoenolpyruvate carboxykinase (ATP) signature. LIGDDEHgWsEdGVfN source prosite : PS00532 40) chain A residue 133 type BINDING sequence F description BINDING => ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1J3B, ECO:0007744|PDB:2PC9 source Swiss-Prot : SWS_FT_FI3 41) chain A residue 216 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P22259 source Swiss-Prot : SWS_FT_FI4 42) chain A residue 232 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9 source Swiss-Prot : SWS_FT_FI5 43) chain A residue 444 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9 source Swiss-Prot : SWS_FT_FI5 44) chain A residue 438 type BINDING sequence R description BINDING => ECO:0000305|PubMed:16239727, ECO:0000305|Ref.3, ECO:0007744|PDB:1XKV, ECO:0007744|PDB:2PC9 source Swiss-Prot : SWS_FT_FI6 45) chain A residue 439 type BINDING sequence F description BINDING => ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:16239727, ECO:0000269|Ref.3 source Swiss-Prot : SWS_FT_FI7

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