eF-site ID 3ujn-A PDB Code 3ujn Chain A click to enlarge Title Formyl Glycinamide Ribonucleotide Amidotransferase from Salmonella Typhimurium : Role of the ATP complexation and glutaminase domain in catalytic coupling Classification LIGASE Compound Phosphoribosylformylglycinamidine synthase Source ORGANISM_SCIENTIFIC: Salmonella enterica subsp. enterica serovar Typhimurium; Sequence A:  GLVPRGSHMMEILRGSPALSAFRINKLLARFQAANLQVHN IYAEYVHFADLNAPLNDSEQAQLTRLLQYGPALSSHTPAG KLLLVTPRPGTISPWSSKATDIAHNCGLQQVDRLERGVAY YIEASTLTAEQWRQVAAELHDRMMETVFSSLTDAEKLFIH HQPAPVSSVDLLGEGRQALIDANLRLGLALAEDEIDYLQE AFTKLGRNPNDIELYMFAQANSEHCRHKIFNADWIIDGKP QPKSLFKMIKNTFETTPDYVLSAYKDNAAVMEGSAVGRYF ADHNTGRYDFHQEPAHILMKVETHNHPTAISPWPGAATGS GGEIRDEGATGRGAKPKAGLVGFSVSNLRIPGFEQPWEED FGKPERIVTALDIMTEGPLGGAAFNNEFGRPALTGYFRTY EEKVNSHNGEELRGYHKPIMLAGGIGNIRADHVQKGEIVV GAKLIVLGGPAMNIGLDFASVQRDNPEMERRCQEVIDRCW QLGDANPILFIHDVGAGGLSNAMPELVSDGGRGGKFELRD ILSDEPGMSPLEIWCNESQERYVLAVAADQLPLFDELCKR ERAPYAVIGDATEEQHLSLHDNHFDNQPIDLPLDVLLGKT PKMTRDVQTLKAKGDALNRADITIADAVKRVLHLPTVAEK TFLVTIGDRTVTGMVARDQMVGPWQVPVADCAVTTASLDS YYGEAMSIGERAPVALLDFAASARLAVGEALTNIAATQIG DIKRIKLSANWMAAAGHPGEDAGLYDAVKAVGEELCPQLG LTIPVGKDSMSMKTRWQEGNEQREMTSPLSLVISAFARVE DVRHTLTPQLSTEDNALLLIDLGKGHNALGATALAQVYRQ LGDKPADVRDVAQLKGFYDAMQALVAARKLLAWHDRSDGG LLVTLAEMAFAGHCGVQVDIAALGDDHLAALFNEELGGVI QVRAEDRDAVEALLAQYGLADCVHYLGQALAGDRFVITAN DQTVFSESRTTLRVWWAETTWQMQRLRDNPQCADQEHEAK ANDTDPGLNVKLSFDINEDIAAPYIATGARPKVAVLREQG VNSHVEMAAAFHRAGFDAIDVHMSDLLGGRIGLGNFHALV ACGGFSYGDVLGAGEGWAKSILFNHRVRDEFETFFHRPQT LALGVXNGCQMMSNLRELIPGSELWPRFVRNHSDRFEARF SLVEVTQSPSLLLQGMVGSQMPIAVSHGEGRVEVRDDAHL AALESKGLVALRYVDNFGKVTETYPANPNGSPNGITAVTT ENGRVTIMMPHPERVFRTVANSWHPENWGEDSPWMRIFRN ARKQLG Description (1)  Phosphoribosylformylglycinamidine synthase (E.C.6.3.5.3) Functional site 1) chain A residue 295 type sequence T description BINDING SITE FOR RESIDUE SO4 A 2002 source : AC1 2) chain A residue 297 type sequence N description BINDING SITE FOR RESIDUE SO4 A 2002 source : AC1 3) chain A residue 298 type sequence H description BINDING SITE FOR RESIDUE SO4 A 2002 source : AC1 4) chain A residue 409 type sequence K description BINDING SITE FOR RESIDUE SO4 A 2002 source : AC1 5) chain A residue 778 type sequence S description BINDING SITE FOR RESIDUE SO4 A 2002 source : AC1 6) chain A residue 333 type sequence V description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 7) chain A residue 386 type sequence T description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 8) chain A residue 387 type sequence G description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 9) chain A residue 388 type sequence Y description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 10) chain A residue 649 type sequence K description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 11) chain A residue 652 type sequence L description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 12) chain A residue 653 type sequence V description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 13) chain A residue 668 type sequence Q description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 14) chain A residue 676 type sequence P description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 15) chain A residue 678 type sequence A description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 16) chain A residue 679 type sequence D description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 17) chain A residue 718 type sequence E description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 18) chain A residue 722 type sequence N description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 19) chain A residue 886 type sequence S description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 20) chain A residue 718 type sequence E description BINDING SITE FOR RESIDUE MG A 2006 source : AC3 21) chain A residue 886 type sequence S description BINDING SITE FOR RESIDUE MG A 2007 source : AC4 22) chain A residue 679 type sequence D description BINDING SITE FOR RESIDUE MG A 2008 source : AC5 23) chain A residue 722 type sequence N description BINDING SITE FOR RESIDUE MG A 2008 source : AC5 24) chain A residue 884 type sequence D description BINDING SITE FOR RESIDUE MG A 2008 source : AC5 25) chain A residue 886 type sequence S description BINDING SITE FOR RESIDUE MG A 2008 source : AC5 26) chain A residue 12 type sequence S description BINDING SITE FOR RESIDUE SO4 A 2009 source : AC6 27) chain A residue 13 type sequence A description BINDING SITE FOR RESIDUE SO4 A 2009 source : AC6 28) chain A residue 14 type sequence F description BINDING SITE FOR RESIDUE SO4 A 2009 source : AC6 29) chain A residue 998 type sequence N description BINDING SITE FOR RESIDUE SO4 A 2009 source : AC6 30) chain A residue 1161 type sequence H description BINDING SITE FOR RESIDUE SO4 A 2009 source : AC6 31) chain A residue 386 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI4 32) chain A residue 678 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI4 33) chain A residue 886 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI4 34) chain A residue 679 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00419, ECO:0000269|PubMed:15301531, ECO:0000269|PubMed:22683785, ECO:0000269|PubMed:24223728 source Swiss-Prot : SWS_FT_FI5 35) chain A residue 718 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00419, ECO:0000269|PubMed:15301531, ECO:0000269|PubMed:22683785, ECO:0000269|PubMed:24223728 source Swiss-Prot : SWS_FT_FI5 36) chain A residue 722 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00419, ECO:0000269|PubMed:15301531, ECO:0000269|PubMed:22683785, ECO:0000269|PubMed:24223728 source Swiss-Prot : SWS_FT_FI5 37) chain A residue 884 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00419, ECO:0000269|PubMed:15301531, ECO:0000269|PubMed:22683785, ECO:0000269|PubMed:24223728 source Swiss-Prot : SWS_FT_FI5 38) chain A residue 307 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00419 source Swiss-Prot : SWS_FT_FI3 39) chain A residue 1135 type ACT_SITE sequence X description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00419 source Swiss-Prot : SWS_FT_FI1 40) chain A residue 1260 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00419 source Swiss-Prot : SWS_FT_FI2 41) chain A residue 1262 type ACT_SITE sequence E description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00419 source Swiss-Prot : SWS_FT_FI2

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