eF-site ID 1cde-D PDB Code 1cde Chain D click to enlarge Title STRUCTURES OF APO AND COMPLEXED ESCHERICHIA COLI GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE Classification TRANSFERASE(FORMYL) Compound PHOSPHORIBOSYL-GLYCINAMIDE FORMYLTRANSFERASE Source Escherichia coli (strain K12) (PUR3_ECOLI) Sequence D:  MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADA FGLERARQAGIATHTLIASAFDSREAYDRELIHEIDMYAP DVVVLAGFMRILSPAFVSHYAGRLLNIHPSLLPKYPGLHT HRQALENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGD SEDDITARVQTQEHAIYPLVISWFADGRLKMHENAAWLDG QRLPPQGYA Description Functional site 1) chain D residue 10 type sequence N description BINDING SITE FOR RESIDUE GAR D 222 source : AC7 2) chain D residue 11 type sequence G description BINDING SITE FOR RESIDUE GAR D 222 source : AC7 3) chain D residue 12 type sequence S description BINDING SITE FOR RESIDUE GAR D 222 source : AC7 4) chain D residue 13 type sequence N description BINDING SITE FOR RESIDUE GAR D 222 source : AC7 5) chain D residue 87 type sequence G description BINDING SITE FOR RESIDUE GAR D 222 source : AC7 6) chain D residue 89 type sequence M description BINDING SITE FOR RESIDUE GAR D 222 source : AC7 7) chain D residue 107 type sequence I description BINDING SITE FOR RESIDUE GAR D 222 source : AC7 8) chain D residue 108 type sequence H description BINDING SITE FOR RESIDUE GAR D 222 source : AC7 9) chain D residue 109 type sequence P description BINDING SITE FOR RESIDUE GAR D 222 source : AC7 10) chain D residue 170 type sequence Q description BINDING SITE FOR RESIDUE GAR D 222 source : AC7 11) chain D residue 173 type sequence E description BINDING SITE FOR RESIDUE GAR D 222 source : AC7 12) chain D residue 89 type sequence M description BINDING SITE FOR RESIDUE DZF D 225 source : AC8 13) chain D residue 90 type sequence R description BINDING SITE FOR RESIDUE DZF D 225 source : AC8 14) chain D residue 91 type sequence I description BINDING SITE FOR RESIDUE DZF D 225 source : AC8 15) chain D residue 92 type sequence L description BINDING SITE FOR RESIDUE DZF D 225 source : AC8 16) chain D residue 97 type sequence V description BINDING SITE FOR RESIDUE DZF D 225 source : AC8 17) chain D residue 106 type sequence N description BINDING SITE FOR RESIDUE DZF D 225 source : AC8 18) chain D residue 139 type sequence V description BINDING SITE FOR RESIDUE DZF D 225 source : AC8 19) chain D residue 140 type sequence T description BINDING SITE FOR RESIDUE DZF D 225 source : AC8 20) chain D residue 141 type sequence D description BINDING SITE FOR RESIDUE DZF D 225 source : AC8 21) chain D residue 142 type sequence E description BINDING SITE FOR RESIDUE DZF D 225 source : AC8 22) chain D residue 144 type sequence D description BINDING SITE FOR RESIDUE DZF D 225 source : AC8 23) chain D 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 24) chain D 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 25) chain D residue 64 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510 source Swiss-Prot : SWS_FT_FI3 26) chain D residue 106 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510 source Swiss-Prot : SWS_FT_FI3 27) chain D 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 28) chain D residue 106 type catalytic sequence N description 363 source MCSA : MCSA4 29) chain D residue 108 type catalytic sequence H description 363 source MCSA : MCSA4 30) chain D residue 135 type catalytic sequence S description 363 source MCSA : MCSA4 31) chain D residue 144 type catalytic sequence D description 363 source MCSA : MCSA4 32) chain D residue 140 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098 source Swiss-Prot : SWS_FT_FI4 33) chain D residue 170 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098 source Swiss-Prot : SWS_FT_FI4 34) chain D 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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