eF-site ID 4dfr-AB PDB Code 4dfr Chain A, B 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 Escherichia coli (strain K12) (DYR_ECOLI) Sequence A:  MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLDKPV IMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDE AIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVE GDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFKILERR B:  MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLDKPV IMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDE AIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVE GDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFKILERR Description Functional site 1) chain A residue 5 type sequence I description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS. source : APT 2) chain A residue 6 type sequence A description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS. source : APT 3) chain A residue 7 type sequence A description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS. source : APT 4) chain A residue 22 type sequence W description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS. source : APT 5) chain A residue 27 type sequence D description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS. source : APT 6) chain A residue 28 type sequence L description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS. source : APT 7) chain A residue 31 type sequence F description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS. source : APT 8) chain A residue 94 type sequence I description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS. source : APT 9) chain A residue 113 type sequence T description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS. source : APT 10) chain A residue 49 type sequence S description RESIDUES INTERACTING WITH THE N(10) METHYL OF THE METHOTREXATE INHIBITOR source : ANM 11) chain A residue 28 type sequence L description RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR source : AAB 12) chain A residue 31 type sequence F description RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR source : AAB 13) chain A residue 50 type sequence I description RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR source : AAB 14) chain A residue 52 type sequence R description RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR source : AAB 15) chain A residue 54 type sequence L description RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR source : AAB 16) chain A residue 28 type sequence L description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : AGL 17) chain A residue 31 type sequence F description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : AGL 18) chain A residue 32 type sequence K description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : AGL 19) chain A residue 54 type sequence L description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : AGL 20) chain A residue 57 type sequence R description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : AGL 21) chain B residue 5 type sequence I description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS. source : BPT 22) chain B residue 6 type sequence A description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS. source : BPT 23) chain B residue 7 type sequence A description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS. source : BPT 24) chain B residue 22 type sequence W description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS. source : BPT 25) chain B residue 27 type sequence D description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS. source : BPT 26) chain B residue 28 type sequence L description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS. source : BPT 27) chain B residue 31 type sequence F description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS. source : BPT 28) chain B residue 94 type sequence I description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS. source : BPT 29) chain B residue 113 type sequence T description RESIDUES INTERACTING WITH THE PTERIDINE OF THE METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT MAIN CHAIN SEGMENTS. source : BPT 30) chain B residue 49 type sequence S description RESIDUES INTERACTING WITH THE N(10) METHYL OF THE METHOTREXATE INHIBITOR source : BNM 31) chain B residue 28 type sequence L description RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR source : BAB 32) chain B residue 31 type sequence F description RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR source : BAB 33) chain B residue 50 type sequence I description RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR source : BAB 34) chain B residue 52 type sequence R description RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR source : BAB 35) chain B residue 54 type sequence L description RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR source : BAB 36) chain B residue 28 type sequence L description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : BGL 37) chain B residue 31 type sequence F description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : BGL 38) chain B residue 32 type sequence K description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : BGL 39) chain B residue 54 type sequence L description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : BGL 40) chain B residue 57 type sequence R description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : BGL 41) chain A residue 43 type sequence G description BINDING SITE FOR RESIDUE CL A 160 source : AC1 42) chain A residue 45 type sequence H description BINDING SITE FOR RESIDUE CL A 160 source : AC1 43) chain A residue 46 type sequence T description BINDING SITE FOR RESIDUE CL A 160 source : AC1 44) chain A residue 96 type sequence G description BINDING SITE FOR RESIDUE CL A 160 source : AC1 45) chain B residue 43 type sequence G description BINDING SITE FOR RESIDUE CL B 160 source : AC2 46) chain B residue 46 type sequence T description BINDING SITE FOR RESIDUE CL B 160 source : AC2 47) chain B residue 96 type sequence G description BINDING SITE FOR RESIDUE CL B 160 source : AC2 48) chain B residue 135 type sequence S description BINDING SITE FOR RESIDUE CA B 161 source : AC3 49) chain A residue 5 type sequence I description BINDING SITE FOR RESIDUE MTX A 161 source : AC4 50) chain A residue 6 type sequence A description BINDING SITE FOR RESIDUE MTX A 161 source : AC4 51) chain A residue 27 type sequence D description BINDING SITE FOR RESIDUE MTX A 161 source : AC4 52) chain A residue 31 type sequence F description BINDING SITE FOR RESIDUE MTX A 161 source : AC4 53) chain A residue 32 type sequence K description BINDING SITE FOR RESIDUE MTX A 161 source : AC4 54) chain A residue 52 type sequence R description BINDING SITE FOR RESIDUE MTX A 161 source : AC4 55) chain A residue 57 type sequence R description BINDING SITE FOR RESIDUE MTX A 161 source : AC4 56) chain A residue 94 type sequence I description BINDING SITE FOR RESIDUE MTX A 161 source : AC4 57) chain A residue 100 type sequence Y description BINDING SITE FOR RESIDUE MTX A 161 source : AC4 58) chain A residue 113 type sequence T description BINDING SITE FOR RESIDUE MTX A 161 source : AC4 59) chain B residue 5 type sequence I description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 60) chain B residue 6 type sequence A description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 61) chain B residue 7 type sequence A description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 62) chain B residue 27 type sequence D description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 63) chain B residue 28 type sequence L description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 64) chain B residue 31 type sequence F description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 65) chain B residue 32 type sequence K description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 66) chain B residue 50 type sequence I description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 67) chain B residue 52 type sequence R description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 68) chain B residue 54 type sequence L description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 69) chain B residue 57 type sequence R description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 70) chain B residue 94 type sequence I description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 71) chain B residue 100 type sequence Y description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 72) chain B residue 113 type sequence T description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 73) chain A residue 13-35 type prosite sequence VIGMENAMPWNLPADLAWFKRNT description DHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGmenaMPWnlpa.DlawFkrnT source prosite : PS00075 74) chain B residue 113 type BINDING sequence T description BINDING => ECO:0000305|PubMed:9012674 source Swiss-Prot : SWS_FT_FI1 75) chain B residue 57 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9012674 source Swiss-Prot : SWS_FT_FI1 76) chain A residue 5 type BINDING sequence I description BINDING => ECO:0000305|PubMed:9012674 source Swiss-Prot : SWS_FT_FI1 77) chain A residue 27 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9012674 source Swiss-Prot : SWS_FT_FI1 78) chain A residue 52 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9012674 source Swiss-Prot : SWS_FT_FI1 79) chain A residue 57 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9012674 source Swiss-Prot : SWS_FT_FI1 80) chain A residue 113 type BINDING sequence T description BINDING => ECO:0000305|PubMed:9012674 source Swiss-Prot : SWS_FT_FI1 81) chain B residue 5 type BINDING sequence I description BINDING => ECO:0000305|PubMed:9012674 source Swiss-Prot : SWS_FT_FI1 82) chain B residue 27 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9012674 source Swiss-Prot : SWS_FT_FI1 83) chain B residue 52 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9012674 source Swiss-Prot : SWS_FT_FI1 84) chain B residue 63 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 85) chain B residue 76 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 86) chain B residue 95 type BINDING sequence G description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 87) chain A residue 45 type BINDING sequence H description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 88) chain A residue 63 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 89) chain A residue 76 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 90) chain A residue 95 type BINDING sequence G description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 91) chain B residue 7 type BINDING sequence A description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 92) chain B residue 13 type BINDING sequence V description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 93) chain B residue 45 type BINDING sequence H description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 94) chain A residue 7 type BINDING sequence A description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 95) chain A residue 13 type BINDING sequence V description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2

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