eF-site ID 1cde-B PDB Code 1cde Chain B 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 B:  MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADA FGLERARQAGIATHTLIASAFDSREAYDRELIHEIDMYAP DVVVLAGFMRILSPAFVSHYAGRLLNIHPSLLPKYPGLHT HRQALENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGD SEDDITARVQTQEHAIYPLVISWFADGRLKMHENAAWLDG QRLPPQGYA Description Functional site 1) chain B residue 10 type sequence N description BINDING SITE FOR RESIDUE GAR B 222 source : AC3 2) chain B residue 11 type sequence G description BINDING SITE FOR RESIDUE GAR B 222 source : AC3 3) chain B residue 12 type sequence S description BINDING SITE FOR RESIDUE GAR B 222 source : AC3 4) chain B residue 13 type sequence N description BINDING SITE FOR RESIDUE GAR B 222 source : AC3 5) chain B residue 87 type sequence G description BINDING SITE FOR RESIDUE GAR B 222 source : AC3 6) chain B residue 89 type sequence M description BINDING SITE FOR RESIDUE GAR B 222 source : AC3 7) chain B residue 107 type sequence I description BINDING SITE FOR RESIDUE GAR B 222 source : AC3 8) chain B residue 108 type sequence H description BINDING SITE FOR RESIDUE GAR B 222 source : AC3 9) chain B residue 109 type sequence P description BINDING SITE FOR RESIDUE GAR B 222 source : AC3 10) chain B residue 170 type sequence Q description BINDING SITE FOR RESIDUE GAR B 222 source : AC3 11) chain B residue 173 type sequence E description BINDING SITE FOR RESIDUE GAR B 222 source : AC3 12) chain B residue 89 type sequence M description BINDING SITE FOR RESIDUE DZF B 225 source : AC4 13) chain B residue 90 type sequence R description BINDING SITE FOR RESIDUE DZF B 225 source : AC4 14) chain B residue 91 type sequence I description BINDING SITE FOR RESIDUE DZF B 225 source : AC4 15) chain B residue 92 type sequence L description BINDING SITE FOR RESIDUE DZF B 225 source : AC4 16) chain B residue 97 type sequence V description BINDING SITE FOR RESIDUE DZF B 225 source : AC4 17) chain B residue 106 type sequence N description BINDING SITE FOR RESIDUE DZF B 225 source : AC4 18) chain B residue 139 type sequence V description BINDING SITE FOR RESIDUE DZF B 225 source : AC4 19) chain B residue 140 type sequence T description BINDING SITE FOR RESIDUE DZF B 225 source : AC4 20) chain B residue 141 type sequence D description BINDING SITE FOR RESIDUE DZF B 225 source : AC4 21) chain B residue 142 type sequence E description BINDING SITE FOR RESIDUE DZF B 225 source : AC4 22) chain B residue 144 type sequence D description BINDING SITE FOR RESIDUE DZF B 225 source : AC4 23) chain B 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 B 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 B 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 B 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 B 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 B residue 106 type catalytic sequence N description 363 source MCSA : MCSA2 29) chain B residue 108 type catalytic sequence H description 363 source MCSA : MCSA2 30) chain B residue 135 type catalytic sequence S description 363 source MCSA : MCSA2 31) chain B residue 144 type catalytic sequence D description 363 source MCSA : MCSA2 32) chain B residue 140 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098 source Swiss-Prot : SWS_FT_FI4 33) chain B residue 170 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098 source Swiss-Prot : SWS_FT_FI4 34) chain B 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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