eF-site ID 6dfr-A PDB Code 6dfr Chain A click to enlarge Title CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE. THE NADP+ HOLOENZYME AND THE FOLATE(DOT)NADP+ TERNARY COMPLEX. SUBSTRATE BINDING AND A MODEL FOR THE TRANSITION STATE Classification OXIDOREDUCTASE Compound DIHYDROFOLATE REDUCTASE Source Escherichia coli (strain K12) (DYR_ECOLI) Sequence A:  MISLIAALAVDRVIGPWNLPADLAWFKRNTLDKPVIMGRH TWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAAC GDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHF PDYEPDDWESVFSEFHDADAQNSHSYCFEILERR Description Functional site 1) chain A residue 94 type sequence I description BINDING SITE FOR RESIDUE CA A 350 source : AC1 2) chain A residue 14 type sequence I description BINDING SITE FOR RESIDUE NAP A 164 source : AC2 3) chain A residue 43 type sequence G description BINDING SITE FOR RESIDUE NAP A 164 source : AC2 4) chain A residue 44 type sequence R description BINDING SITE FOR RESIDUE NAP A 164 source : AC2 5) chain A residue 45 type sequence H description BINDING SITE FOR RESIDUE NAP A 164 source : AC2 6) chain A residue 46 type sequence T description BINDING SITE FOR RESIDUE NAP A 164 source : AC2 7) chain A residue 62 type sequence L description BINDING SITE FOR RESIDUE NAP A 164 source : AC2 8) chain A residue 63 type sequence S description BINDING SITE FOR RESIDUE NAP A 164 source : AC2 9) chain A residue 64 type sequence S description BINDING SITE FOR RESIDUE NAP A 164 source : AC2 10) chain A residue 76 type sequence K description BINDING SITE FOR RESIDUE NAP A 164 source : AC2 11) chain A residue 96 type sequence G description BINDING SITE FOR RESIDUE NAP A 164 source : AC2 12) chain A residue 97 type sequence G description BINDING SITE FOR RESIDUE NAP A 164 source : AC2 13) chain A residue 98 type sequence R description BINDING SITE FOR RESIDUE NAP A 164 source : AC2 14) chain A residue 99 type sequence V description BINDING SITE FOR RESIDUE NAP A 164 source : AC2 15) chain A residue 102 type sequence Q description BINDING SITE FOR RESIDUE NAP A 164 source : AC2 16) chain A residue 123 type sequence T description BINDING SITE FOR RESIDUE NAP A 164 source : AC2 17) chain A residue 13-35 type prosite sequence VIGPWNLPADLAWFKRNT description DHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGmenaMPWnlpa.DlawFkrnT source prosite : PS00075 18) chain A residue 113 type BINDING sequence T description BINDING => ECO:0000305|PubMed:9012674 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 5 type BINDING sequence I description BINDING => ECO:0000305|PubMed:9012674 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 27 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9012674 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 52 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9012674 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 57 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9012674 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 13 type BINDING sequence V description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 24) chain A residue 45 type BINDING sequence H description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 25) chain A residue 63 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 76 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 95 type BINDING sequence G description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 7 type BINDING sequence A description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2

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