eF-site ID 1f28-ABCD PDB Code 1f28 Chain A, B, C, D click to enlarge Title CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE FROM PNEUMOCYSTIS CARINII BOUND TO DUMP AND BW1843U89 Classification TRANSFERASE Compound THYMIDYLATE SYNTHASE Source Pneumocystis carinii (TYSY_PNECA) Sequence A:  NAEEQQYLNLVQYIINHGEDRPDRTGTGTLSVFAPSPLKF SLRNKTFPLLTTKRVFIRGVIEELLWFIRGETDSLKLREK NIHIWDANGSREYLDSIGLTKRQEGDLGPIYGFQWRHFGA EYIDCKTNYIGQGVDQLANIIQKIRTSPYDRRLILSAWNP ADLEKMALPPCHMFCQFYVHIPSNNHRPELSCQLYQRSCD MGLGVPFNIASYALLTCMIAHVCDLDPGDFIHVMGDCHIY KDHIEALQQQLTRSPRPFPTLSLNRSITDIEDFTLDDFNI QNYHPYETIKMKMSI B:  NAEEQQYLNLVQYIINHGEDRPDRTGTGTLSVFAPSPLKF SLRNKTFPLLTTKRVFIRGVIEELLWFIRGETDSLKLREK NIHIWDANGSREYLDSIGLTKRQEGDLGPIYGFQWRHFGA EYIDCKTNYIGQGVDQLANIIQKIRTSPYDRRLILSAWNP ADLEKMALPPCHMFCQFYVHIPSNNHRPELSCQLYQRSCD MGLGVPFNIASYALLTCMIAHVCDLDPGDFIHVMGDCHIY KDHIEALQQQLTRSPRPFPTLSLNRSITDIEDFTLDDFNI QNYHPYETIKMKMSI C:  NAEEQQYLNLVQYIINHGEDRPDRTGTGTLSVFAPSPLKF SLRNKTFPLLTTKRVFIRGVIEELLWFIRGETDSLKLREK NIHIWDANGSREYLDSIGLTKRQEGDLGPIYGFQWRHFGA EYIDCKTNYIGQGVDQLANIIQKIRTSPYDRRLILSAWNP ADLEKMALPPCHMFCQFYVHIPSNNHRPELSCQLYQRSCD MGLGVPFNIASYALLTCMIAHVCDLDPGDFIHVMGDCHIY KDHIEALQQQLTRSPRPFPTLSLNRSITDIEDFTLDDFNI QNYHPYETIKMKMSI D:  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 A residue 26 type sequence R description BINDING SITE FOR RESIDUE UMP A 301 source : AC1 2) chain A residue 170 type sequence L description BINDING SITE FOR RESIDUE UMP A 301 source : AC1 3) chain A residue 173 type sequence C description BINDING SITE FOR RESIDUE UMP A 301 source : AC1 4) chain A residue 174 type sequence H description BINDING SITE FOR RESIDUE UMP A 301 source : AC1 5) chain A residue 198 type sequence Q description BINDING SITE FOR RESIDUE UMP A 301 source : AC1 6) chain A residue 199 type sequence R description BINDING SITE FOR RESIDUE UMP A 301 source : AC1 7) chain A residue 200 type sequence S description BINDING SITE FOR RESIDUE UMP A 301 source : AC1 8) chain A residue 202 type sequence D description BINDING SITE FOR RESIDUE UMP A 301 source : AC1 9) chain A residue 206 type sequence G description BINDING SITE FOR RESIDUE UMP A 301 source : AC1 10) chain A residue 210 type sequence N description BINDING SITE FOR RESIDUE UMP A 301 source : AC1 11) chain A residue 240 type sequence H description BINDING SITE FOR RESIDUE UMP A 301 source : AC1 12) chain A residue 242 type sequence Y description BINDING SITE FOR RESIDUE UMP A 301 source : AC1 13) chain B residue 153 type sequence R description BINDING SITE FOR RESIDUE UMP A 301 source : AC1 14) chain B residue 154 type sequence R description BINDING SITE FOR RESIDUE UMP A 301 source : AC1 15) chain A residue 153 type sequence R description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 16) chain A residue 154 type sequence R description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 17) chain B residue 26 type sequence R description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 18) chain B residue 170 type sequence L description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 19) chain B residue 173 type sequence C description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 20) chain B residue 174 type sequence H description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 21) chain B residue 198 type sequence Q description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 22) chain B residue 199 type sequence R description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 23) chain B residue 200 type sequence S description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 24) chain B residue 202 type sequence D description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 25) chain B residue 210 type sequence N description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 26) chain B residue 240 type sequence H description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 27) chain B residue 242 type sequence Y description BINDING SITE FOR RESIDUE UMP B 302 source : AC2 28) chain C residue 26 type sequence R description BINDING SITE FOR RESIDUE UMP C 303 source : AC3 29) chain C residue 113 type sequence Y description BINDING SITE FOR RESIDUE UMP C 303 source : AC3 30) chain C residue 170 type sequence L description BINDING SITE FOR RESIDUE UMP C 303 source : AC3 31) chain C residue 173 type sequence C description BINDING SITE FOR RESIDUE UMP C 303 source : AC3 32) chain C residue 174 type sequence H description BINDING SITE FOR RESIDUE UMP C 303 source : AC3 33) chain C residue 198 type sequence Q description BINDING SITE FOR RESIDUE UMP C 303 source : AC3 34) chain C residue 199 type sequence R description BINDING SITE FOR RESIDUE UMP C 303 source : AC3 35) chain C residue 200 type sequence S description BINDING SITE FOR RESIDUE UMP C 303 source : AC3 36) chain C residue 202 type sequence D description BINDING SITE FOR RESIDUE UMP C 303 source : AC3 37) chain C residue 206 type sequence G description BINDING SITE FOR RESIDUE UMP C 303 source : AC3 38) chain C residue 210 type sequence N description BINDING SITE FOR RESIDUE UMP C 303 source : AC3 39) chain C residue 240 type sequence H description BINDING SITE FOR RESIDUE UMP C 303 source : AC3 40) chain C residue 242 type sequence Y description BINDING SITE FOR RESIDUE UMP C 303 source : AC3 41) chain D residue 153 type sequence R description BINDING SITE FOR RESIDUE UMP C 303 source : AC3 42) chain D residue 154 type sequence R description BINDING SITE FOR RESIDUE UMP C 303 source : AC3 43) chain C residue 153 type sequence R description BINDING SITE FOR RESIDUE UMP D 304 source : AC4 44) chain C residue 154 type sequence R description BINDING SITE FOR RESIDUE UMP D 304 source : AC4 45) chain D residue 26 type sequence R description BINDING SITE FOR RESIDUE UMP D 304 source : AC4 46) chain D residue 170 type sequence L description BINDING SITE FOR RESIDUE UMP D 304 source : AC4 47) chain D residue 173 type sequence C description BINDING SITE FOR RESIDUE UMP D 304 source : AC4 48) chain D residue 174 type sequence H description BINDING SITE FOR RESIDUE UMP D 304 source : AC4 49) chain D residue 198 type sequence Q description BINDING SITE FOR RESIDUE UMP D 304 source : AC4 50) chain D residue 199 type sequence R description BINDING SITE FOR RESIDUE UMP D 304 source : AC4 51) chain D residue 200 type sequence S description BINDING SITE FOR RESIDUE UMP D 304 source : AC4 52) chain D residue 202 type sequence D description BINDING SITE FOR RESIDUE UMP D 304 source : AC4 53) chain D residue 210 type sequence N description BINDING SITE FOR RESIDUE UMP D 304 source : AC4 54) chain D residue 240 type sequence H description BINDING SITE FOR RESIDUE UMP D 304 source : AC4 55) chain D residue 242 type sequence Y description BINDING SITE FOR RESIDUE UMP D 304 source : AC4 56) chain A residue 58 type sequence F description BINDING SITE FOR RESIDUE F89 A 401 source : AC5 57) chain A residue 61 type sequence G description BINDING SITE FOR RESIDUE F89 A 401 source : AC5 58) chain A residue 65 type sequence E description BINDING SITE FOR RESIDUE F89 A 401 source : AC5 59) chain A residue 85 type sequence H description BINDING SITE FOR RESIDUE F89 A 401 source : AC5 60) chain A residue 86 type sequence I description BINDING SITE FOR RESIDUE F89 A 401 source : AC5 61) chain A residue 87 type sequence W description BINDING SITE FOR RESIDUE F89 A 401 source : AC5 62) chain A residue 90 type sequence N description BINDING SITE FOR RESIDUE F89 A 401 source : AC5 63) chain A residue 170 type sequence L description BINDING SITE FOR RESIDUE F89 A 401 source : AC5 64) chain A residue 202 type sequence D description BINDING SITE FOR RESIDUE F89 A 401 source : AC5 65) chain A residue 205 type sequence L description BINDING SITE FOR RESIDUE F89 A 401 source : AC5 66) chain A residue 206 type sequence G description BINDING SITE FOR RESIDUE F89 A 401 source : AC5 67) chain A residue 209 type sequence F description BINDING SITE FOR RESIDUE F89 A 401 source : AC5 68) chain A residue 296 type sequence S description BINDING SITE FOR RESIDUE F89 A 401 source : AC5 69) chain B residue 58 type sequence F description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 70) chain B residue 61 type sequence G description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 71) chain B residue 65 type sequence E description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 72) chain B residue 85 type sequence H description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 73) chain B residue 86 type sequence I description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 74) chain B residue 87 type sequence W description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 75) chain B residue 90 type sequence N description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 76) chain B residue 202 type sequence D description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 77) chain B residue 206 type sequence G description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 78) chain B residue 209 type sequence F description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 79) chain B residue 242 type sequence Y description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 80) chain B residue 295 type sequence M description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 81) chain B residue 297 type sequence I description BINDING SITE FOR RESIDUE F89 B 402 source : AC6 82) chain C residue 58 type sequence F description BINDING SITE FOR RESIDUE F89 C 403 source : AC7 83) chain C residue 61 type sequence G description BINDING SITE FOR RESIDUE F89 C 403 source : AC7 84) chain C residue 65 type sequence E description BINDING SITE FOR RESIDUE F89 C 403 source : AC7 85) chain C residue 85 type sequence H description BINDING SITE FOR RESIDUE F89 C 403 source : AC7 86) chain C residue 86 type sequence I description BINDING SITE FOR RESIDUE F89 C 403 source : AC7 87) chain C residue 87 type sequence W description BINDING SITE FOR RESIDUE F89 C 403 source : AC7 88) chain C residue 90 type sequence N description BINDING SITE FOR RESIDUE F89 C 403 source : AC7 89) chain C residue 170 type sequence L description BINDING SITE FOR RESIDUE F89 C 403 source : AC7 90) chain C residue 202 type sequence D description BINDING SITE FOR RESIDUE F89 C 403 source : AC7 91) chain C residue 205 type sequence L description BINDING SITE FOR RESIDUE F89 C 403 source : AC7 92) chain C residue 206 type sequence G description BINDING SITE FOR RESIDUE F89 C 403 source : AC7 93) chain C residue 209 type sequence F description BINDING SITE FOR RESIDUE F89 C 403 source : AC7 94) chain C residue 242 type sequence Y description BINDING SITE FOR RESIDUE F89 C 403 source : AC7 95) chain C residue 296 type sequence S description BINDING SITE FOR RESIDUE F89 C 403 source : AC7 96) chain D residue 58 type sequence F description BINDING SITE FOR RESIDUE F89 D 404 source : AC8 97) chain D residue 61 type sequence G description BINDING SITE FOR RESIDUE F89 D 404 source : AC8 98) chain D residue 65 type sequence E description BINDING SITE FOR RESIDUE F89 D 404 source : AC8 99) chain D residue 85 type sequence H description BINDING SITE FOR RESIDUE F89 D 404 source : AC8 100) chain D residue 86 type sequence I description BINDING SITE FOR RESIDUE F89 D 404 source : AC8 101) chain D residue 87 type sequence W description BINDING SITE FOR RESIDUE F89 D 404 source : AC8 102) chain D residue 90 type sequence N description BINDING SITE FOR RESIDUE F89 D 404 source : AC8 103) chain D residue 202 type sequence D description BINDING SITE FOR RESIDUE F89 D 404 source : AC8 104) chain D residue 206 type sequence G description BINDING SITE FOR RESIDUE F89 D 404 source : AC8 105) chain D residue 209 type sequence F description BINDING SITE FOR RESIDUE F89 D 404 source : AC8 106) chain D residue 242 type sequence Y description BINDING SITE FOR RESIDUE F89 D 404 source : AC8 107) chain D residue 295 type sequence M description BINDING SITE FOR RESIDUE F89 D 404 source : AC8 108) chain D residue 297 type sequence I description BINDING SITE FOR RESIDUE F89 D 404 source : AC8 109) chain A residue 173 type ACT_SITE sequence C description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 110) chain B residue 173 type ACT_SITE sequence C description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 111) chain C residue 173 type ACT_SITE sequence C description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 112) chain D residue 173 type ACT_SITE sequence C description Nucleophile => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI1 113) chain A residue 26 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 114) chain C residue 199 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 115) chain C residue 210 type BINDING sequence N description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 116) chain C residue 240 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 117) chain D residue 26 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 118) chain D residue 199 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 119) chain D residue 210 type BINDING sequence N description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 120) chain D residue 240 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 121) chain A residue 199 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 122) chain A residue 210 type BINDING sequence N description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 123) chain A residue 240 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 124) chain B residue 26 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 125) chain B residue 199 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 126) chain B residue 210 type BINDING sequence N description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 127) chain B residue 240 type BINDING sequence H description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 128) chain C residue 26 type BINDING sequence R description in other chain => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI2 129) chain A residue 153 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI3 130) chain A residue 202 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI3 131) chain B residue 153 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI3 132) chain B residue 202 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI3 133) chain C residue 153 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI3 134) chain C residue 202 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI3 135) chain D residue 153 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI3 136) chain D residue 202 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P0A884 source Swiss-Prot : SWS_FT_FI3 137) chain A residue 153-181 type prosite sequence RRLILSAWNPADLEKMALPPCHMFCQFYV description THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RrlIlsaWNpadlekma.....LpPCHmfcQFyV source prosite : PS00091

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