eF-site ID 1cde-C PDB Code 1cde Chain C 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 C:  MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADA FGLERARQAGIATHTLIASAFDSREAYDRELIHEIDMYAP DVVVLAGFMRILSPAFVSHYAGRLLNIHPSLLPKYPGLHT HRQALENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGD SEDDITARVQTQEHAIYPLVISWFADGRLKMHENAAWLDG QRLPPQGYA Description Functional site 1) chain C residue 10 type sequence N description BINDING SITE FOR RESIDUE GAR C 222 source : AC5 2) chain C residue 11 type sequence G description BINDING SITE FOR RESIDUE GAR C 222 source : AC5 3) chain C residue 12 type sequence S description BINDING SITE FOR RESIDUE GAR C 222 source : AC5 4) chain C residue 13 type sequence N description BINDING SITE FOR RESIDUE GAR C 222 source : AC5 5) chain C residue 87 type sequence G description BINDING SITE FOR RESIDUE GAR C 222 source : AC5 6) chain C residue 89 type sequence M description BINDING SITE FOR RESIDUE GAR C 222 source : AC5 7) chain C residue 107 type sequence I description BINDING SITE FOR RESIDUE GAR C 222 source : AC5 8) chain C residue 108 type sequence H description BINDING SITE FOR RESIDUE GAR C 222 source : AC5 9) chain C residue 109 type sequence P description BINDING SITE FOR RESIDUE GAR C 222 source : AC5 10) chain C residue 170 type sequence Q description BINDING SITE FOR RESIDUE GAR C 222 source : AC5 11) chain C residue 173 type sequence E description BINDING SITE FOR RESIDUE GAR C 222 source : AC5 12) chain C residue 89 type sequence M description BINDING SITE FOR RESIDUE DZF C 225 source : AC6 13) chain C residue 90 type sequence R description BINDING SITE FOR RESIDUE DZF C 225 source : AC6 14) chain C residue 91 type sequence I description BINDING SITE FOR RESIDUE DZF C 225 source : AC6 15) chain C residue 92 type sequence L description BINDING SITE FOR RESIDUE DZF C 225 source : AC6 16) chain C residue 97 type sequence V description BINDING SITE FOR RESIDUE DZF C 225 source : AC6 17) chain C residue 106 type sequence N description BINDING SITE FOR RESIDUE DZF C 225 source : AC6 18) chain C residue 139 type sequence V description BINDING SITE FOR RESIDUE DZF C 225 source : AC6 19) chain C residue 140 type sequence T description BINDING SITE FOR RESIDUE DZF C 225 source : AC6 20) chain C residue 141 type sequence D description BINDING SITE FOR RESIDUE DZF C 225 source : AC6 21) chain C residue 142 type sequence E description BINDING SITE FOR RESIDUE DZF C 225 source : AC6 22) chain C residue 144 type sequence D description BINDING SITE FOR RESIDUE DZF C 225 source : AC6 23) chain C residue 106 type catalytic sequence N description 363 source MCSA : MCSA3 24) chain C residue 108 type catalytic sequence H description 363 source MCSA : MCSA3 25) chain C residue 135 type catalytic sequence S description 363 source MCSA : MCSA3 26) chain C residue 144 type catalytic sequence D description 363 source MCSA : MCSA3 27) chain C 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 C 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 29) chain C 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 30) chain C residue 64 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510 source Swiss-Prot : SWS_FT_FI3 31) chain C residue 106 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510 source Swiss-Prot : SWS_FT_FI3 32) chain C residue 140 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098 source Swiss-Prot : SWS_FT_FI4 33) chain C residue 170 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098 source Swiss-Prot : SWS_FT_FI4 34) chain C 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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