eF-site ID 6nkj-B PDB Code 6nkj Chain 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 B:  MDKIVVQGGDNRLVGSVTIEGAKNAVLPLLAATILASEGK TVLQNVPILSDVFIMNQVVGGLNAKVDFDEEAHLVKVDAT GDITEEAPYKYVSKMRASIVVLGPILARVGHAKVSMPGGC TIGSRPIDLHLKGLEAMGVKISQTAGYIEAKAERLHGAHI YMDFPSVGATQNLMMAATLADGVTVIENAAREPEIVDLAI LLNEMGAKVKGAGTETITITGVEKLHGTTHNVVQDRIEAG TFMVAAAMTGGDVLIRDAVWEHNRPLIAKLLEMGVEVIEE DEGIRVRSQLENLKAVHVKTLPHPGFPTDMQAQFTALMTV AKGESTMVETVFENRFQHLEEMRRMGLHSEIIRDTARIVG GQPLQGAEVLSTDLRASAALILTGLVAQGETVVGKLVHLD RGYYGFHEKLAQLGAKIQRIE Description Functional site 1) chain B residue 344 type sequence R description binding site for residue CL A 503 source : AC3 2) chain B residue 226 type sequence H description binding site for residue EDO B 502 source : AC4 3) chain B residue 299 type sequence K description binding site for residue EDO B 502 source : AC4 4) chain B residue 23 type sequence K description binding site for residue CIT B 503 source : AC5 5) chain B residue 24 type sequence N description binding site for residue CIT B 503 source : AC5 6) chain B residue 122 type sequence I description binding site for residue CIT B 503 source : AC5 7) chain B residue 125 type sequence R description binding site for residue CIT B 503 source : AC5 8) chain B residue 309 type sequence D description binding site for residue CIT B 503 source : AC5 9) chain B residue 332 type sequence F description binding site for residue CIT B 503 source : AC5 10) chain B residue 335 type sequence R description binding site for residue CIT B 503 source : AC5 11) chain B residue 374 type sequence L description binding site for residue CIT B 503 source : AC5 12) chain B residue 375 type sequence R description binding site for residue CIT B 503 source : AC5 13) chain B residue 401 type sequence R description binding site for residue CIT B 503 source : AC5 14) chain B residue 203 type sequence N description binding site for residue CL B 504 source : AC6 15) chain B residue 96 type sequence R description binding site for Di-peptide 0V5 B 501 and CYS B 120 source : AC7 16) chain B residue 119 type sequence G description binding site for Di-peptide 0V5 B 501 and CYS B 120 source : AC7 17) chain B residue 121 type sequence T description binding site for Di-peptide 0V5 B 501 and CYS B 120 source : AC7 18) chain B residue 122 type sequence I description binding site for Di-peptide 0V5 B 501 and CYS B 120 source : AC7 19) chain B residue 123 type sequence G description binding site for Di-peptide 0V5 B 501 and CYS B 120 source : AC7 20) chain B residue 125 type sequence R description binding site for Di-peptide 0V5 B 501 and CYS B 120 source : AC7 21) chain B residue 401 type sequence R description binding site for Di-peptide 0V5 B 501 and CYS B 120 source : AC7 22) chain B residue 120 type ACT_SITE sequence C description Proton donor => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI1 23) chain B residue 331 type BINDING sequence V description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI2 24) chain B residue 23 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI2 25) chain B residue 96 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI2 26) chain B residue 125 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI2 27) chain B residue 309 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00111 source Swiss-Prot : SWS_FT_FI2 28) 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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