eF-site ID 4dfr-B PDB Code 4dfr Chain 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 B:  MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLDKPV IMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDE AIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVE GDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFKILERR Description Functional site 1) 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 2) 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 3) 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 4) 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 5) 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 6) 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 7) 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 8) 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 9) 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 10) chain B residue 49 type sequence S description RESIDUES INTERACTING WITH THE N(10) METHYL OF THE METHOTREXATE INHIBITOR source : BNM 11) chain B residue 28 type sequence L description RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR source : BAB 12) chain B residue 31 type sequence F description RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR source : BAB 13) chain B residue 50 type sequence I description RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR source : BAB 14) chain B residue 52 type sequence R description RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR source : BAB 15) chain B residue 54 type sequence L description RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF THE METHOTREXATE INHIBITOR source : BAB 16) chain B residue 28 type sequence L description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : BGL 17) chain B residue 31 type sequence F description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : BGL 18) chain B residue 32 type sequence K description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : BGL 19) chain B residue 54 type sequence L description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : BGL 20) chain B residue 57 type sequence R description RESIDUES INTERACTING WITH THE GLUTAMATE OF THE METHOTREXATE INHIBITOR source : BGL 21) chain B residue 43 type sequence G description BINDING SITE FOR RESIDUE CL B 160 source : AC2 22) chain B residue 46 type sequence T description BINDING SITE FOR RESIDUE CL B 160 source : AC2 23) chain B residue 96 type sequence G description BINDING SITE FOR RESIDUE CL B 160 source : AC2 24) chain B residue 135 type sequence S description BINDING SITE FOR RESIDUE CA B 161 source : AC3 25) chain B residue 5 type sequence I description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 26) chain B residue 6 type sequence A description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 27) chain B residue 7 type sequence A description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 28) chain B residue 27 type sequence D description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 29) chain B residue 28 type sequence L description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 30) chain B residue 31 type sequence F description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 31) chain B residue 32 type sequence K description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 32) chain B residue 50 type sequence I description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 33) chain B residue 52 type sequence R description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 34) chain B residue 54 type sequence L description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 35) chain B residue 57 type sequence R description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 36) chain B residue 94 type sequence I description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 37) chain B residue 100 type sequence Y description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 38) chain B residue 113 type sequence T description BINDING SITE FOR RESIDUE MTX B 162 source : AC5 39) chain B residue 113 type BINDING sequence T description BINDING => ECO:0000305|PubMed:9012674 source Swiss-Prot : SWS_FT_FI1 40) chain B residue 5 type BINDING sequence I description BINDING => ECO:0000305|PubMed:9012674 source Swiss-Prot : SWS_FT_FI1 41) chain B residue 27 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9012674 source Swiss-Prot : SWS_FT_FI1 42) chain B residue 52 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9012674 source Swiss-Prot : SWS_FT_FI1 43) chain B residue 57 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9012674 source Swiss-Prot : SWS_FT_FI1 44) chain B residue 63 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 45) chain B residue 76 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 46) chain B residue 95 type BINDING sequence G description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 47) chain B residue 7 type BINDING sequence A description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 48) chain B residue 13 type BINDING sequence V description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2 49) chain B residue 45 type BINDING sequence H description BINDING => ECO:0000269|PubMed:19374017 source Swiss-Prot : SWS_FT_FI2

Display surface Download Links