eF-site ID 1f28-B PDB Code 1f28 Chain B click to enlarge Title CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE FROM PNEUMOCYSTIS CARINII BOUND TO DUMP AND BW1843U89 Classification TRANSFERASE Compound THYMIDYLATE SYNTHASE Source null (TYSY_PNECA) Sequence B:  NAEEQQYLNLVQYIINHGEDRPDRTGTGTLSVFAPSPLKF SLRNKTFPLLTTKRVFIRGVIEELLWFIRGETDSLKLREK NIHIWDANGSREYLDSIGLTKRQEGDLGPIYGFQWRHFGA EYIDCKTNYIGQGVDQLANIIQKIRTSPYDRRLILSAWNP ADLEKMALPPCHMFCQFYVHIPSNNHRPELSCQLYQRSCD MGLGVPFNIASYALLTCMIAHVCDLDPGDFIHVMGDCHIY KDHIEALQQQLTRSPRPFPTLSLNRSITDIEDFTLDDFNI QNYHPYETIKMKMSI Description (1)  THYMIDYLATE SYNTHASE (E.C. 2.1.1.45) FROM PNEUMOCYSTIS CARINII BOUND TO DUMP AND BW1843U89 Functional site 1) chain B residue 153 type sequence R description BINDING SITE FOR RESIDUE UMP A 301 source : AC1 2) chain B residue 154 type sequence R description BINDING SITE FOR RESIDUE UMP A 301 source : AC1 3) chain B residue 26 type sequence R description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 4) chain B residue 170 type sequence L description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 5) chain B residue 173 type sequence C description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 6) chain B residue 174 type sequence H description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 7) chain B residue 198 type sequence Q description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 8) chain B residue 199 type sequence R description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 9) chain B residue 200 type sequence S description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 10) chain B residue 202 type sequence D description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 11) chain B residue 210 type sequence N description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 12) chain B residue 240 type sequence H description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 13) chain B residue 242 type sequence Y description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 14) chain B residue 58 type sequence F description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 15) chain B residue 61 type sequence G description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 16) chain B residue 65 type sequence E description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 17) chain B residue 85 type sequence H description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 18) chain B residue 86 type sequence I description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 19) chain B residue 87 type sequence W description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 20) chain B residue 90 type sequence N description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 21) chain B residue 202 type sequence D description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 22) chain B residue 206 type sequence G description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 23) chain B residue 209 type sequence F description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 24) chain B residue 242 type sequence Y description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 25) chain B residue 295 type sequence M description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 26) chain B residue 297 type sequence I description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 27) chain B residue 173 type ACT_SITE sequence C description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 26 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 29) chain B residue 199 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 30) chain B residue 210 type BINDING sequence N description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 31) chain B residue 240 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 32) chain B residue 153 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI3 33) chain B residue 202 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI3

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