eF-site ID 6nkj-AB PDB Code 6nkj Chain A, B click to enlarge Title 1.3 Angstrom Resolution Crystal Structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase from Streptococcus pneumoniae in Complex with (2R)-2-(phosphonooxy)propanoic acid. Classification TRANSFERASE Compound UDP-N-acetylglucosamine 1-carboxyvinyltransferase 1 Source (MURA1_STRPN) Sequence A:  MDKIVVQGGDNRLVGSVTIEGAKNAVLPLLAATILASEGK TVLQNVPILSDVFIMNQVVGGLNAKVDFDEEAHLVKVDAT GDITEEAPYKYVSKMRASIVVLGPILARVGHAKVSMPGGC TIGSRPIDLHLKGLEAMGVKISQTAGYIEAKAERLHGAHI YMDFPSVGATQNLMMAATLADGVTVIENAAREPEIVDLAI LLNEMGAKVKGAGTETITITGVEKLHGTTHNVVQDRIEAG TFMVAAAMTGGDVLIRDAVWEHNRPLIAKLLEMGVEVIEE DEGIRVRSQLENLKAVHVKTLPHPGFPTDMQAQFTALMTV AKGESTMVETVFENRFQHLEEMRRMGLHSEIIRDTARIVG GQPLQGAEVLSTDLRASAALILTGLVAQGETVVGKLVHLD RGYYGFHEKLAQLGAKIQRIE B:  MDKIVVQGGDNRLVGSVTIEGAKNAVLPLLAATILASEGK TVLQNVPILSDVFIMNQVVGGLNAKVDFDEEAHLVKVDAT GDITEEAPYKYVSKMRASIVVLGPILARVGHAKVSMPGGC TIGSRPIDLHLKGLEAMGVKISQTAGYIEAKAERLHGAHI YMDFPSVGATQNLMMAATLADGVTVIENAAREPEIVDLAI LLNEMGAKVKGAGTETITITGVEKLHGTTHNVVQDRIEAG TFMVAAAMTGGDVLIRDAVWEHNRPLIAKLLEMGVEVIEE DEGIRVRSQLENLKAVHVKTLPHPGFPTDMQAQFTALMTV AKGESTMVETVFENRFQHLEEMRRMGLHSEIIRDTARIVG GQPLQGAEVLSTDLRASAALILTGLVAQGETVVGKLVHLD RGYYGFHEKLAQLGAKIQRIE Description Functional site 1) chain A residue 96 type sequence R description binding site for residue 0V5 A 501 source : AC1 2) chain A residue 120 type sequence C description binding site for residue 0V5 A 501 source : AC1 3) chain A residue 121 type sequence T description binding site for residue 0V5 A 501 source : AC1 4) chain A residue 401 type sequence R description binding site for residue 0V5 A 501 source : AC1 5) chain A residue 23 type sequence K description binding site for residue CIT A 502 source : AC2 6) chain A residue 24 type sequence N description binding site for residue CIT A 502 source : AC2 7) chain A residue 122 type sequence I description binding site for residue CIT A 502 source : AC2 8) chain A residue 125 type sequence R description binding site for residue CIT A 502 source : AC2 9) chain A residue 309 type sequence D description binding site for residue CIT A 502 source : AC2 10) chain A residue 335 type sequence R description binding site for residue CIT A 502 source : AC2 11) chain A residue 374 type sequence L description binding site for residue CIT A 502 source : AC2 12) chain A residue 375 type sequence R description binding site for residue CIT A 502 source : AC2 13) chain A residue 401 type sequence R description binding site for residue CIT A 502 source : AC2 14) chain A residue 115 type sequence S description binding site for residue CL A 503 source : AC3 15) chain A residue 146 type sequence G description binding site for residue CL A 503 source : AC3 16) chain A residue 147 type sequence Y description binding site for residue CL A 503 source : AC3 17) chain B residue 344 type sequence R description binding site for residue CL A 503 source : AC3 18) chain B residue 226 type sequence H description binding site for residue EDO B 502 source : AC4 19) chain B residue 299 type sequence K description binding site for residue EDO B 502 source : AC4 20) chain B residue 23 type sequence K description binding site for residue CIT B 503 source : AC5 21) chain B residue 24 type sequence N description binding site for residue CIT B 503 source : AC5 22) chain B residue 122 type sequence I description binding site for residue CIT B 503 source : AC5 23) chain B residue 125 type sequence R description binding site for residue CIT B 503 source : AC5 24) chain B residue 309 type sequence D description binding site for residue CIT B 503 source : AC5 25) chain B residue 332 type sequence F description binding site for residue CIT B 503 source : AC5 26) chain B residue 335 type sequence R description binding site for residue CIT B 503 source : AC5 27) chain B residue 374 type sequence L description binding site for residue CIT B 503 source : AC5 28) chain B residue 375 type sequence R description binding site for residue CIT B 503 source : AC5 29) chain B residue 401 type sequence R description binding site for residue CIT B 503 source : AC5 30) chain B residue 203 type sequence N description binding site for residue CL B 504 source : AC6 31) chain A residue 340 type sequence E description binding site for Di-peptide 0V5 B 501 and CYS B 120 source : AC7 32) chain B residue 96 type sequence R description binding site for Di-peptide 0V5 B 501 and CYS B 120 source : AC7 33) chain B residue 119 type sequence G description binding site for Di-peptide 0V5 B 501 and CYS B 120 source : AC7 34) chain B residue 121 type sequence T description binding site for Di-peptide 0V5 B 501 and CYS B 120 source : AC7 35) chain B residue 122 type sequence I description binding site for Di-peptide 0V5 B 501 and CYS B 120 source : AC7 36) chain B residue 123 type sequence G description binding site for Di-peptide 0V5 B 501 and CYS B 120 source : AC7 37) chain B residue 125 type sequence R description binding site for Di-peptide 0V5 B 501 and CYS B 120 source : AC7 38) chain B residue 401 type sequence R description binding site for Di-peptide 0V5 B 501 and CYS B 120 source : AC7 39) chain A residue 120 type ACT_SITE sequence C description Proton donor => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI1 40) chain B residue 120 type ACT_SITE sequence C description Proton donor => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI1 41) chain A residue 23 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI2 42) chain B residue 331 type BINDING sequence V description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI2 43) chain A residue 96 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 125 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI2 45) chain A residue 309 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI2 46) chain A residue 331 type BINDING sequence V description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI2 47) chain B residue 23 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI2 48) chain B residue 96 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI2 49) chain B residue 125 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI2 50) chain B residue 309 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI2 51) chain A residue 120 type MOD_RES sequence C description 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI3 52) chain B residue 120 type MOD_RES sequence C description 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI3

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