eF-site ID 1s3v-A PDB Code 1s3v Chain A click to enlarge Title Structure Determination of Tetrahydroquinazoline Antifolates in Complex with Human and Pneumocystis carinii Dihydrofolate Reductase: Correlations of Enzyme Selectivity and Stereochemistry Classification OXIDOREDUCTASE Compound Dihydrofolate reductase Source Homo sapiens (Human) (DYR_HUMAN) Sequence A:  VGSLNCIVAVSQNMGIGKNGDLPWPPLRNEFRYFQRMTTT SSVEGKQNLVIMGKKTWFSIPEKNRPLKGRINLVLSRELK EPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSSV YKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLP EYPGVLSDVQEEKGIKYKFEVYEKND Description (1)  Dihydrofolate reductase (E.C.1.5.1.3) Functional site 1) chain A residue 53 type sequence G description BINDING SITE FOR RESIDUE SO4 A 188 source : AC1 2) chain A residue 54 type sequence K description BINDING SITE FOR RESIDUE SO4 A 188 source : AC1 3) chain A residue 55 type sequence K description BINDING SITE FOR RESIDUE SO4 A 188 source : AC1 4) chain A residue 56 type sequence T description BINDING SITE FOR RESIDUE SO4 A 188 source : AC1 5) chain A residue 117 type sequence G description BINDING SITE FOR RESIDUE SO4 A 188 source : AC1 6) chain A residue 120 type sequence V description BINDING SITE FOR RESIDUE SO4 A 188 source : AC1 7) chain A residue 76 type sequence S description BINDING SITE FOR RESIDUE SO4 A 189 source : AC2 8) chain A residue 77 type sequence R description BINDING SITE FOR RESIDUE SO4 A 189 source : AC2 9) chain A residue 78 type sequence E description BINDING SITE FOR RESIDUE SO4 A 189 source : AC2 10) chain A residue 7 type sequence I description BINDING SITE FOR RESIDUE TQD A 187 source : AC3 11) chain A residue 8 type sequence V description BINDING SITE FOR RESIDUE TQD A 187 source : AC3 12) chain A residue 9 type sequence A description BINDING SITE FOR RESIDUE TQD A 187 source : AC3 13) chain A residue 21 type sequence D description BINDING SITE FOR RESIDUE TQD A 187 source : AC3 14) chain A residue 30 type sequence E description BINDING SITE FOR RESIDUE TQD A 187 source : AC3 15) chain A residue 31 type sequence F description BINDING SITE FOR RESIDUE TQD A 187 source : AC3 16) chain A residue 34 type sequence F description BINDING SITE FOR RESIDUE TQD A 187 source : AC3 17) chain A residue 35 type sequence Q description BINDING SITE FOR RESIDUE TQD A 187 source : AC3 18) chain A residue 61 type sequence P description BINDING SITE FOR RESIDUE TQD A 187 source : AC3 19) chain A residue 64 type sequence N description BINDING SITE FOR RESIDUE TQD A 187 source : AC3 20) chain A residue 115 type sequence V description BINDING SITE FOR RESIDUE TQD A 187 source : AC3 21) chain A residue 121 type sequence Y description BINDING SITE FOR RESIDUE TQD A 187 source : AC3 22) chain A residue 136 type sequence T description BINDING SITE FOR RESIDUE TQD A 187 source : AC3 23) chain A residue 23 type catalytic sequence P description 490 source MCSA : MCSA1 24) chain A residue 31 type catalytic sequence F description 490 source MCSA : MCSA1 25) chain A residue 31 type BINDING sequence F description BINDING => ECO:0000305|PubMed:2248959 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 65 type BINDING sequence R description BINDING => ECO:0000305|PubMed:2248959 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 71 type BINDING sequence I description BINDING => ECO:0000305|PubMed:2248959 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 10 type BINDING sequence V description BINDING => ECO:0000269|PubMed:15039552, ECO:0000269|PubMed:16222560, ECO:0000269|PubMed:19478082 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 16 type BINDING sequence I description BINDING => ECO:0000269|PubMed:15039552, ECO:0000269|PubMed:16222560, ECO:0000269|PubMed:19478082 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 55 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15039552, ECO:0000269|PubMed:16222560, ECO:0000269|PubMed:19478082 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 77 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15039552, ECO:0000269|PubMed:16222560, ECO:0000269|PubMed:19478082 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 117 type BINDING sequence G description BINDING => ECO:0000269|PubMed:15039552, ECO:0000269|PubMed:16222560, ECO:0000269|PubMed:19478082 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 15-38 type prosite sequence GIGKNGDLPWPPLRNEFRYFQRMT description DHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGkngdLPWpplrnEfryFqrmT source prosite : PS00075

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