eF-site ID 3dfr-A PDB Code 3dfr Chain A click to enlarge Title CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS CASEI DIHYDROFOLATE REDUCTASE REFINED AT 1.7 ANGSTROMS RESOLUTION. I. GENERAL FEATURES AND BINDING OF METHOTREXATE Classification OXIDOREDUCTASE Compound DIHYDROFOLATE REDUCTASE Source Lactobacillus casei (DYR_LACCA) Sequence A:  TAFLWAQNRNGLIGKDGHLPWHLPDDLHYFRAQTVGKIMV VGRRTYESFPKRPLPERTNVVLTHQEDYQAQGAVVVHDVA AVFAYAKQHLDQELVIAGGAQIFTAFKDDVDTLLVTRLAG SFEGDTKMIPLNWDDFTKVSSRTVEDTNPALTHTYEVWQK KA Description Functional site 1) chain A residue 62 type sequence L description RESIDUES INTERACTING WITH THE ADENINE BASE OF THE NADPH COFACTOR source : NDN 2) chain A residue 63 type sequence T description RESIDUES INTERACTING WITH THE ADENINE BASE OF THE NADPH COFACTOR source : NDN 3) chain A residue 64 type sequence H description RESIDUES INTERACTING WITH THE ADENINE BASE OF THE NADPH COFACTOR source : NDN 4) chain A residue 77 type sequence H description RESIDUES INTERACTING WITH THE ADENINE BASE OF THE NADPH COFACTOR source : NDN 5) chain A residue 101 type sequence Q description RESIDUES INTERACTING WITH THE ADENINE BASE OF THE NADPH COFACTOR source : NDN 6) chain A residue 102 type sequence I description RESIDUES INTERACTING WITH THE ADENINE BASE OF THE NADPH COFACTOR source : NDN 7) chain A residue 42 type sequence G description RESIDUES INTERACTING WITH THE ADENINE MONONUCLEOTIDE RIBOSE OF THE NADPH COFACTOR source : NAR 8) chain A residue 43 type sequence R description RESIDUES INTERACTING WITH THE ADENINE MONONUCLEOTIDE RIBOSE OF THE NADPH COFACTOR source : NAR 9) chain A residue 44 type sequence R description RESIDUES INTERACTING WITH THE ADENINE MONONUCLEOTIDE RIBOSE OF THE NADPH COFACTOR source : NAR 10) chain A residue 63 type sequence T description RESIDUES INTERACTING WITH THE ADENINE MONONUCLEOTIDE RIBOSE OF THE NADPH COFACTOR source : NAR 11) chain A residue 64 type sequence H description RESIDUES INTERACTING WITH THE ADENINE MONONUCLEOTIDE RIBOSE OF THE NADPH COFACTOR source : NAR 12) chain A residue 65 type sequence Q description RESIDUES INTERACTING WITH THE ADENINE MONONUCLEOTIDE RIBOSE OF THE NADPH COFACTOR source : NAR 13) chain A residue 101 type sequence Q description RESIDUES INTERACTING WITH THE ADENINE MONONUCLEOTIDE RIBOSE OF THE NADPH COFACTOR source : NAR 14) chain A residue 102 type sequence I description RESIDUES INTERACTING WITH THE ADENINE MONONUCLEOTIDE RIBOSE OF THE NADPH COFACTOR source : NAR 15) chain A residue 44 type sequence R description RESIDUES INTERACTING WITH THE PYROPHOSPHATE OF THE NADPH COFACTOR source : NPP 16) chain A residue 45 type sequence T description RESIDUES INTERACTING WITH THE PYROPHOSPHATE OF THE NADPH COFACTOR source : NPP 17) chain A residue 99 type sequence G description RESIDUES INTERACTING WITH THE PYROPHOSPHATE OF THE NADPH COFACTOR source : NPP 18) chain A residue 101 type sequence Q description RESIDUES INTERACTING WITH THE PYROPHOSPHATE OF THE NADPH COFACTOR source : NPP 19) chain A residue 102 type sequence I description RESIDUES INTERACTING WITH THE PYROPHOSPHATE OF THE NADPH COFACTOR source : NPP 20) chain A residue 126 type sequence T description RESIDUES INTERACTING WITH THE PYROPHOSPHATE OF THE NADPH COFACTOR source : NPP 21) chain A residue 13 type sequence I description RESIDUES INTERACTING WITH THE NICOTINAMIDE MONONUCLEOTIDE RIBOSE OF THE NADPH COFACTOR source : NMR 22) chain A residue 14 type sequence G description RESIDUES INTERACTING WITH THE NICOTINAMIDE MONONUCLEOTIDE RIBOSE OF THE NADPH COFACTOR source : NMR 23) chain A residue 18 type sequence H description RESIDUES INTERACTING WITH THE NICOTINAMIDE MONONUCLEOTIDE RIBOSE OF THE NADPH COFACTOR source : NMR 24) chain A residue 48 type sequence S description RESIDUES INTERACTING WITH THE NICOTINAMIDE MONONUCLEOTIDE RIBOSE OF THE NADPH COFACTOR source : NMR 25) chain A residue 99 type sequence G description RESIDUES INTERACTING WITH THE NICOTINAMIDE MONONUCLEOTIDE RIBOSE OF THE NADPH COFACTOR source : NMR 26) chain A residue 5 type sequence W description RESIDUES INTERACTING WITH THE NICOTINAMIDE BASE OF THE NADPH COFACTOR source : NND 27) chain A residue 6 type sequence A description RESIDUES INTERACTING WITH THE NICOTINAMIDE BASE OF THE NADPH COFACTOR source : NND 28) chain A residue 13 type sequence I description RESIDUES INTERACTING WITH THE NICOTINAMIDE BASE OF THE NADPH COFACTOR source : NND 29) chain A residue 19 type sequence L description RESIDUES INTERACTING WITH THE NICOTINAMIDE BASE OF THE NADPH COFACTOR source : NND 30) chain A residue 21 type sequence W description RESIDUES INTERACTING WITH THE NICOTINAMIDE BASE OF THE NADPH COFACTOR source : NND 31) chain A residue 45 type sequence T description RESIDUES INTERACTING WITH THE NICOTINAMIDE BASE OF THE NADPH COFACTOR source : NND 32) chain A residue 97 type sequence A description RESIDUES INTERACTING WITH THE NICOTINAMIDE BASE OF THE NADPH COFACTOR source : NND 33) chain A residue 98 type sequence G description RESIDUES INTERACTING WITH THE NICOTINAMIDE BASE OF THE NADPH COFACTOR source : NND 34) chain A residue 99 type sequence G description RESIDUES INTERACTING WITH THE NICOTINAMIDE BASE OF THE NADPH COFACTOR source : NND 35) chain A residue 103 type sequence F description RESIDUES INTERACTING WITH THE NICOTINAMIDE BASE OF THE NADPH COFACTOR source : NND 36) chain A residue 4 type sequence L description RESIDUES INTERACTING WITH THE PTERIDINE of THE METHOTREXATE INHIBITOR source : MPT 37) chain A residue 5 type sequence W description RESIDUES INTERACTING WITH THE PTERIDINE of THE METHOTREXATE INHIBITOR source : MPT 38) chain A residue 6 type sequence A description RESIDUES INTERACTING WITH THE PTERIDINE of THE METHOTREXATE INHIBITOR source : MPT 39) chain A residue 19 type sequence L description RESIDUES INTERACTING WITH THE PTERIDINE of THE METHOTREXATE INHIBITOR source : MPT 40) chain A residue 21 type sequence W description RESIDUES INTERACTING WITH THE PTERIDINE of THE METHOTREXATE INHIBITOR source : MPT 41) chain A residue 26 type sequence D description RESIDUES INTERACTING WITH THE PTERIDINE of THE METHOTREXATE INHIBITOR source : MPT 42) chain A residue 27 type sequence L description RESIDUES INTERACTING WITH THE PTERIDINE of THE METHOTREXATE INHIBITOR source : MPT 43) chain A residue 30 type sequence F description RESIDUES INTERACTING WITH THE PTERIDINE of THE METHOTREXATE INHIBITOR source : MPT 44) chain A residue 97 type sequence A description RESIDUES INTERACTING WITH THE PTERIDINE of THE METHOTREXATE INHIBITOR source : MPT 45) chain A residue 116 type sequence T description RESIDUES INTERACTING WITH THE PTERIDINE of THE METHOTREXATE INHIBITOR source : MPT 46) chain A residue 19 type sequence L description RESIDUES INTERACTING WITH THE N(10) METHYL OF THE METHOTREXATE INHIBITOR source : MNM 47) chain A residue 48 type sequence S description RESIDUES INTERACTING WITH THE N(10) METHYL OF THE METHOTREXATE INHIBITOR source : MNM 48) chain A residue 27 type sequence L description RESIDUES INTERACTING WITH THE P-AMINOBENZOYL OF THE METHOTREXATE INHIBITOR source : MAB 49) chain A residue 30 type sequence F description RESIDUES INTERACTING WITH THE P-AMINOBENZOYL OF THE METHOTREXATE INHIBITOR source : MAB 50) chain A residue 49 type sequence F description RESIDUES INTERACTING WITH THE P-AMINOBENZOYL OF THE METHOTREXATE INHIBITOR source : MAB 51) chain A residue 50 type sequence P description RESIDUES INTERACTING WITH THE P-AMINOBENZOYL OF THE METHOTREXATE INHIBITOR source : MAB 52) chain A residue 54 type sequence L description RESIDUES INTERACTING WITH THE P-AMINOBENZOYL OF THE METHOTREXATE INHIBITOR source : MAB 53) chain A residue 27 type sequence L description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : MGL 54) chain A residue 28 type sequence H description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : MGL 55) chain A residue 30 type sequence F description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : MGL 56) chain A residue 31 type sequence R description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : MGL 57) chain A residue 54 type sequence L description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : MGL 58) chain A residue 57 type sequence R description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : MGL 59) chain A residue 5 type sequence W description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 60) chain A residue 6 type sequence A description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 61) chain A residue 13 type sequence I description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 62) chain A residue 14 type sequence G description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 63) chain A residue 15 type sequence K description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 64) chain A residue 17 type sequence G description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 65) chain A residue 18 type sequence H description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 66) chain A residue 19 type sequence L description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 67) chain A residue 42 type sequence G description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 68) chain A residue 43 type sequence R description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 69) chain A residue 44 type sequence R description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 70) chain A residue 45 type sequence T description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 71) chain A residue 62 type sequence L description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 72) chain A residue 63 type sequence T description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 73) chain A residue 64 type sequence H description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 74) chain A residue 65 type sequence Q description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 75) chain A residue 77 type sequence H description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 76) chain A residue 97 type sequence A description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 77) chain A residue 99 type sequence G description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 78) chain A residue 100 type sequence A description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 79) chain A residue 101 type sequence Q description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 80) chain A residue 102 type sequence I description BINDING SITE FOR RESIDUE NDP A 163 source : AC1 81) chain A residue 4 type sequence L description BINDING SITE FOR RESIDUE MTX A 164 source : AC2 82) chain A residue 5 type sequence W description BINDING SITE FOR RESIDUE MTX A 164 source : AC2 83) chain A residue 19 type sequence L description BINDING SITE FOR RESIDUE MTX A 164 source : AC2 84) chain A residue 26 type sequence D description BINDING SITE FOR RESIDUE MTX A 164 source : AC2 85) chain A residue 27 type sequence L description BINDING SITE FOR RESIDUE MTX A 164 source : AC2 86) chain A residue 28 type sequence H description BINDING SITE FOR RESIDUE MTX A 164 source : AC2 87) chain A residue 30 type sequence F description BINDING SITE FOR RESIDUE MTX A 164 source : AC2 88) chain A residue 31 type sequence R description BINDING SITE FOR RESIDUE MTX A 164 source : AC2 89) chain A residue 48 type sequence S description BINDING SITE FOR RESIDUE MTX A 164 source : AC2 90) chain A residue 49 type sequence F description BINDING SITE FOR RESIDUE MTX A 164 source : AC2 91) chain A residue 50 type sequence P description BINDING SITE FOR RESIDUE MTX A 164 source : AC2 92) chain A residue 57 type sequence R description BINDING SITE FOR RESIDUE MTX A 164 source : AC2 93) chain A residue 97 type sequence A description BINDING SITE FOR RESIDUE MTX A 164 source : AC2 94) chain A residue 116 type sequence T description BINDING SITE FOR RESIDUE MTX A 164 source : AC2 95) chain A residue 5 type catalytic sequence W description 112 source MCSA : MCSA1 96) chain A residue 20 type catalytic sequence P description 112 source MCSA : MCSA1 97) chain A residue 22 type catalytic sequence H description 112 source MCSA : MCSA1 98) chain A residue 27 type catalytic sequence L description 112 source MCSA : MCSA1 99) chain A residue 28 type catalytic sequence H description 112 source MCSA : MCSA1 100) chain A residue 31 type catalytic sequence R description 112 source MCSA : MCSA1 101) chain A residue 55 type catalytic sequence P description 112 source MCSA : MCSA1 102) chain A residue 95 type catalytic sequence V description 112 source MCSA : MCSA1 103) chain A residue 117 type catalytic sequence R description 112 source MCSA : MCSA1 104) chain A residue 12-34 type prosite sequence LIGKDGHLPWHLPDDLHYFRAQT description DHFR_1 Dihydrofolate reductase (DHFR) domain signature. LIGkdghLPWhlpd.DlhyFraqT source prosite : PS00075 105) chain A residue 5 type BINDING sequence W description BINDING => ECO:0000305|PubMed:6815179 source Swiss-Prot : SWS_FT_FI1 106) chain A residue 27 type BINDING sequence L description BINDING => ECO:0000305|PubMed:6815179 source Swiss-Prot : SWS_FT_FI1 107) chain A residue 32 type BINDING sequence A description BINDING => ECO:0000305|PubMed:6815179 source Swiss-Prot : SWS_FT_FI1 108) chain A residue 58 type BINDING sequence T description BINDING => ECO:0000305|PubMed:6815179 source Swiss-Prot : SWS_FT_FI1 109) chain A residue 117 type BINDING sequence R description BINDING => ECO:0000305|PubMed:6815179 source Swiss-Prot : SWS_FT_FI1 110) chain A residue 6 type BINDING sequence A description BINDING => ECO:0000269|PubMed:6815179 source Swiss-Prot : SWS_FT_FI2 111) chain A residue 14 type BINDING sequence G description BINDING => ECO:0000269|PubMed:6815179 source Swiss-Prot : SWS_FT_FI2 112) chain A residue 43 type BINDING sequence R description BINDING => ECO:0000269|PubMed:6815179 source Swiss-Prot : SWS_FT_FI2 113) chain A residue 63 type BINDING sequence T description BINDING => ECO:0000269|PubMed:6815179 source Swiss-Prot : SWS_FT_FI2 114) chain A residue 80 type BINDING sequence A description BINDING => ECO:0000269|PubMed:6815179 source Swiss-Prot : SWS_FT_FI2 115) chain A residue 98 type BINDING sequence G description BINDING => ECO:0000269|PubMed:6815179 source Swiss-Prot : SWS_FT_FI2 116) chain A residue 22 type SITE sequence H description May be important for enzyme function source Swiss-Prot : SWS_FT_FI3

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