eF-site ID 1c3e-A PDB Code 1c3e Chain A click to enlarge Title NEW INSIGHTS INTO INHIBITOR DESIGN FROM THE CRYSTAL STRUCTURE AND NMR STUDIES OF E. COLI GAR TRANSFORMYLATE IN COMPLEX WITH BETA-GAR AND 10-FORMYL-5,8,10-TRIDEAZAFOLIC ACID. Classification TRANSFERASE Compound GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE Source null (1C3E) Sequence A:  MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADA FGLERARQAGIATHTLIASAFDSREAYDRELIHEIDMYAP DVVVLAGFMRILSPAFVSHYAGRLLNIHPSLLPKYPGLHT HRQALENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGD SEDDITARVQTQEHAIYPLVISWFADGRLKMHENAAWLDG QRLPPQGYA Description Functional site 1) chain A residue 64 type sequence R description BINDING SITE FOR RESIDUE NHR A 220 source : AC1 2) chain A residue 88 type sequence F description BINDING SITE FOR RESIDUE NHR A 220 source : AC1 3) chain A residue 89 type sequence M description BINDING SITE FOR RESIDUE NHR A 220 source : AC1 4) chain A residue 90 type sequence R description BINDING SITE FOR RESIDUE NHR A 220 source : AC1 5) chain A residue 91 type sequence I description BINDING SITE FOR RESIDUE NHR A 220 source : AC1 6) chain A residue 92 type sequence L description BINDING SITE FOR RESIDUE NHR A 220 source : AC1 7) chain A residue 97 type sequence V description BINDING SITE FOR RESIDUE NHR A 220 source : AC1 8) chain A residue 106 type sequence N description BINDING SITE FOR RESIDUE NHR A 220 source : AC1 9) chain A residue 108 type sequence H description BINDING SITE FOR RESIDUE NHR A 220 source : AC1 10) chain A residue 118 type sequence L description BINDING SITE FOR RESIDUE NHR A 220 source : AC1 11) chain A residue 139 type sequence V description BINDING SITE FOR RESIDUE NHR A 220 source : AC1 12) chain A residue 140 type sequence T description BINDING SITE FOR RESIDUE NHR A 220 source : AC1 13) chain A residue 142 type sequence E description BINDING SITE FOR RESIDUE NHR A 220 source : AC1 14) chain A residue 143 type sequence L description BINDING SITE FOR RESIDUE NHR A 220 source : AC1 15) chain A residue 144 type sequence D description BINDING SITE FOR RESIDUE NHR A 220 source : AC1 16) chain A residue 11 type sequence G description BINDING SITE FOR RESIDUE GAR A 221 source : AC2 17) chain A residue 12 type sequence S description BINDING SITE FOR RESIDUE GAR A 221 source : AC2 18) chain A residue 13 type sequence N description BINDING SITE FOR RESIDUE GAR A 221 source : AC2 19) chain A residue 87 type sequence G description BINDING SITE FOR RESIDUE GAR A 221 source : AC2 20) chain A residue 88 type sequence F description BINDING SITE FOR RESIDUE GAR A 221 source : AC2 21) chain A residue 89 type sequence M description BINDING SITE FOR RESIDUE GAR A 221 source : AC2 22) chain A residue 107 type sequence I description BINDING SITE FOR RESIDUE GAR A 221 source : AC2 23) chain A residue 109 type sequence P description BINDING SITE FOR RESIDUE GAR A 221 source : AC2 24) chain A residue 173 type sequence E description BINDING SITE FOR RESIDUE GAR A 221 source : AC2 25) chain A residue 131 type sequence E description BINDING SITE FOR RESIDUE NHR B 222 source : AC3 26) chain A residue 106 type catalytic sequence N description 363 source MCSA : MCSA1 27) chain A residue 108 type catalytic sequence H description 363 source MCSA : MCSA1 28) chain A residue 135 type catalytic sequence S description 363 source MCSA : MCSA1 29) chain A residue 144 type catalytic sequence D description 363 source MCSA : MCSA1 30) chain A residue 108 type ACT_SITE sequence H description Proton donor => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10433709 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 11 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 89 type BINDING sequence M description BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098 source Swiss-Prot : SWS_FT_FI2 33) chain A residue 106 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 64 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510 source Swiss-Prot : SWS_FT_FI3 35) chain A residue 133-156 type prosite sequence GTSVHFVTDELDGGPVILQAKVPV description GART Phosphoribosylglycinamide formyltransferase active site. GtSVhFVtDeLDgGpvIlqakvpV source prosite : PS00373 36) chain A residue 140 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098 source Swiss-Prot : SWS_FT_FI4 37) chain A residue 170 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098 source Swiss-Prot : SWS_FT_FI4 38) chain A residue 144 type SITE sequence D description Raises pKa of active site His => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10433709 source Swiss-Prot : SWS_FT_FI5

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