eF-site ID 1m9n-A PDB Code 1m9n Chain A click to enlarge Title CRYSTAL STRUCTURE OF THE HOMODIMERIC BIFUNCTIONAL TRANSFORMYLASE AND CYCLOHYDROLASE ENZYME AVIAN ATIC IN COMPLEX WITH AICAR AND XMP AT 1.93 ANGSTROMS. Classification transferase, hydrolase Compound AICAR TRANSFORMYLASE-IMP CYCLOHYDROLASE Source null (PUR9_CHICK) Sequence A:  RQQLALLSVSEKAGLVEFARSLNALGLGLIASGGTATALR DAGLPVRDVSDLTGFPEMLGGRVKTLHPAVHAGILARNIP EDNADMNKQDFSLVRVVVCNLYPFVKTVSSPGVTVPEAVE KIDIGGVALLRAAAKNHARVTVVCDPADYSSVAKEMAASK DKDTSVETRRHLALKAFTHTAQYDAAISDYFRKEYSKGVS QLPLRYGMNPHQSPAQLYTTRPKLPLTVVNGSPGFINLCD ALNAWQLVKELKQALGIPAAASFKHVSPAGAAVGIPLSEE EAQVCMVHDLHKTLTPLASAYARSRGADRMSSFGDFIALS DICDVPTAKIISREVSDGVVAPGYEEEALKILSKKKNGGY CVLQMDPNYEPDDNEIRTLYGLQLMQKRNNAVIDRSLFKN IVTKNKTLPESAVRDLIVASIAVKYTQSNSVCYAKDGQVI GIGAGQQSRIHCTRLAGDKANSWWLRHHPRVLSMKFKAGV KRAEVSNAIDQYVTGTIGEDEDLVKWQAMFEEVPAQLTEA EKKQWIAKLTAVSLSSDAFFPFRDNVDRAKRIGVQFIVAP SGSAADEVVIEACNELGITLIHTNLRLFHH Description Functional site 1) chain A residue 426 type sequence V description BINDING SITE FOR RESIDUE K A 594 source : AC1 2) chain A residue 429 type sequence T description BINDING SITE FOR RESIDUE K A 594 source : AC1 3) chain A residue 431 type sequence S description BINDING SITE FOR RESIDUE K A 594 source : AC1 4) chain A residue 433 type sequence S description BINDING SITE FOR RESIDUE K A 594 source : AC1 5) chain A residue 540 type sequence D description BINDING SITE FOR RESIDUE K A 594 source : AC1 6) chain A residue 590 type sequence L description BINDING SITE FOR RESIDUE K A 594 source : AC1 7) chain A residue 592 type sequence H description BINDING SITE FOR RESIDUE K A 594 source : AC1 8) chain A residue 208 type sequence R description BINDING SITE FOR RESIDUE AMZ A 1001 source : AC3 9) chain A residue 209 type sequence Y description BINDING SITE FOR RESIDUE AMZ A 1001 source : AC3 10) chain A residue 239 type sequence I description BINDING SITE FOR RESIDUE AMZ A 1001 source : AC3 11) chain A residue 240 type sequence N description BINDING SITE FOR RESIDUE AMZ A 1001 source : AC3 12) chain A residue 267 type sequence K description BINDING SITE FOR RESIDUE AMZ A 1001 source : AC3 13) chain A residue 268 type sequence H description BINDING SITE FOR RESIDUE AMZ A 1001 source : AC3 14) chain A residue 317 type sequence G description BINDING SITE FOR RESIDUE AMZ A 1001 source : AC3 15) chain A residue 340 type sequence D description BINDING SITE FOR RESIDUE AMZ A 1001 source : AC3 16) chain A residue 542 type sequence F description BINDING SITE FOR RESIDUE AMZ B 1002 source : AC4 17) chain A residue 589 type sequence R description BINDING SITE FOR RESIDUE AMZ B 1002 source : AC4 18) chain A residue 11 type sequence S description BINDING SITE FOR RESIDUE XMP A 1003 source : AC5 19) chain A residue 12 type sequence V description BINDING SITE FOR RESIDUE XMP A 1003 source : AC5 20) chain A residue 13 type sequence S description BINDING SITE FOR RESIDUE XMP A 1003 source : AC5 21) chain A residue 15 type sequence K description BINDING SITE FOR RESIDUE XMP A 1003 source : AC5 22) chain A residue 35 type sequence S description BINDING SITE FOR RESIDUE XMP A 1003 source : AC5 23) chain A residue 37 type sequence G description BINDING SITE FOR RESIDUE XMP A 1003 source : AC5 24) chain A residue 38 type sequence T description BINDING SITE FOR RESIDUE XMP A 1003 source : AC5 25) chain A residue 64 type sequence G description BINDING SITE FOR RESIDUE XMP A 1003 source : AC5 26) chain A residue 65 type sequence R description BINDING SITE FOR RESIDUE XMP A 1003 source : AC5 27) chain A residue 67 type sequence K description BINDING SITE FOR RESIDUE XMP A 1003 source : AC5 28) chain A residue 68 type sequence T description BINDING SITE FOR RESIDUE XMP A 1003 source : AC5 29) chain A residue 69 type sequence L description BINDING SITE FOR RESIDUE XMP A 1003 source : AC5 30) chain A residue 102 type sequence C description BINDING SITE FOR RESIDUE XMP A 1003 source : AC5 31) chain A residue 103 type sequence N description BINDING SITE FOR RESIDUE XMP A 1003 source : AC5 32) chain A residue 104 type sequence L description BINDING SITE FOR RESIDUE XMP A 1003 source : AC5 33) chain A residue 105 type sequence Y description BINDING SITE FOR RESIDUE XMP A 1003 source : AC5 34) chain A residue 126 type sequence D description BINDING SITE FOR RESIDUE XMP A 1003 source : AC5 35) chain A residue 127 type sequence I description BINDING SITE FOR RESIDUE XMP A 1003 source : AC5 36) chain A residue 128 type sequence G description BINDING SITE FOR RESIDUE XMP A 1003 source : AC5 37) chain A residue 129 type sequence G description BINDING SITE FOR RESIDUE XMP A 1003 source : AC5 38) chain A residue 138 type ACT_SITE sequence K description Proton donor/acceptor; for FAICAR cyclization activity => ECO:0000250|UniProtKB:P31939 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 200 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P31939 source Swiss-Prot : SWS_FT_FI10 40) chain A residue 102 type BINDING sequence C description BINDING => ECO:0000305|PubMed:12501179, ECO:0007744|PDB:1M9N source Swiss-Prot : SWS_FT_FI4 41) chain A residue 268 type ACT_SITE sequence H description Proton acceptor; for AICAR formyltransferase activity => ECO:0000250|UniProtKB:P31939 source Swiss-Prot : SWS_FT_FI2 42) chain A residue 13 type BINDING sequence S description BINDING => ECO:0000305|PubMed:11323713, ECO:0000305|PubMed:12501179, ECO:0007744|PDB:1G8M, ECO:0007744|PDB:1M9N source Swiss-Prot : SWS_FT_FI3 43) chain A residue 35 type BINDING sequence S description BINDING => ECO:0000305|PubMed:11323713, ECO:0000305|PubMed:12501179, ECO:0007744|PDB:1G8M, ECO:0007744|PDB:1M9N source Swiss-Prot : SWS_FT_FI3 44) chain A residue 65 type BINDING sequence R description BINDING => ECO:0000305|PubMed:11323713, ECO:0000305|PubMed:12501179, ECO:0007744|PDB:1G8M, ECO:0007744|PDB:1M9N source Swiss-Prot : SWS_FT_FI3 45) chain A residue 126 type BINDING sequence D description BINDING => ECO:0000305|PubMed:11323713, ECO:0000305|PubMed:12501179, ECO:0007744|PDB:1G8M, ECO:0007744|PDB:1M9N source Swiss-Prot : SWS_FT_FI3 46) chain A residue 340 type BINDING sequence D description in other chain => ECO:0000269|PubMed:12501179, ECO:0007744|PDB:1M9N source Swiss-Prot : SWS_FT_FI5 47) chain A residue 208 type BINDING sequence R description in other chain => ECO:0000269|PubMed:12501179, ECO:0007744|PDB:1M9N source Swiss-Prot : SWS_FT_FI5 48) chain A residue 268 type BINDING sequence H description in other chain => ECO:0000269|PubMed:12501179, ECO:0007744|PDB:1M9N source Swiss-Prot : SWS_FT_FI5 49) chain A residue 317 type BINDING sequence G description in other chain => ECO:0000269|PubMed:12501179, ECO:0007744|PDB:1M9N source Swiss-Prot : SWS_FT_FI5 50) chain A residue 452 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P31939 source Swiss-Prot : SWS_FT_FI6 51) chain A residue 432 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P31939 source Swiss-Prot : SWS_FT_FI6 52) chain A residue 566 type BINDING sequence S description BINDING => ECO:0000305|PubMed:12974624, ECO:0007744|PDB:1OZ0 source Swiss-Prot : SWS_FT_FI7 53) chain A residue 547 type BINDING sequence D description BINDING => ECO:0000305|PubMed:12974624, ECO:0007744|PDB:1OZ0 source Swiss-Prot : SWS_FT_FI7 54) chain A residue 453 type BINDING sequence I description BINDING => ECO:0000305|PubMed:12974624, ECO:0007744|PDB:1OZ0 source Swiss-Prot : SWS_FT_FI7 55) chain A residue 542 type BINDING sequence F description BINDING => ECO:0000269|PubMed:12501179, ECO:0007744|PDB:1M9N source Swiss-Prot : SWS_FT_FI8 56) chain A residue 589 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12501179, ECO:0007744|PDB:1M9N source Swiss-Prot : SWS_FT_FI8 57) chain A residue 267 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P31939 source Swiss-Prot : SWS_FT_FI9

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