eF-site ID 3ldv-AB PDB Code 3ldv Chain A, B click to enlarge Title 1.77 Angstrom resolution crystal structure of orotidine 5'-phosphate decarboxylase from Vibrio cholerae O1 biovar eltor str. N16961 Classification LYASE Compound Orotidine 5'-phosphate decarboxylase Source Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) (PYRF_VIBCH) Sequence A:  AMNDPKVIVALDYDNLADALAFVDKIDPSTCRLKVGKEMF TLFGPDFVRELHKRGFSVFLDLKFHDIPNTCSKAVKAAAE LGVWMVNVHASGGERMMAASREILEPYGKERPLLIGVTVL TSMESADLQGIGILSAPQDHVLRLATLTKNAGLDGVVCSA QEASLLKQHLGREFKLVTPGIRPAGSEQGDQRRIMTPAQA IASGSDYLVIGRPITQAAHPEVVLEEINSSL B:  NDPKVIVALDYDNLADALAFVDKIDPSTCRLKVGKEMFTL FGPDFVRELHKRGFSVFLDLKFHDIPNTCSKAVKAAAELG VWMVNVHASGGERMMAASREILEPYGKERPLLIGVTVLTS MESADLQGIGILSAPQDHVLRLATLTKNAGLDGVVCSAQE ASLLKQHLGREFKLVTPGIRPAQRRIMTPAQAIASGSDYL VIGRPITQAAHPEVVLEEINSSLV Description Functional site 1) chain A residue 26 type sequence D description BINDING SITE FOR RESIDUE MG A 232 source : AC1 2) chain A residue 67 type sequence P description BINDING SITE FOR RESIDUE CL A 233 source : AC2 3) chain A residue 68 type sequence N description BINDING SITE FOR RESIDUE CL A 233 source : AC2 4) chain A residue 25 type sequence I description BINDING SITE FOR RESIDUE CL A 234 source : AC3 5) chain A residue 26 type sequence D description BINDING SITE FOR RESIDUE CL A 234 source : AC3 6) chain A residue 29 type sequence T description BINDING SITE FOR RESIDUE CL A 234 source : AC3 7) chain A residue 220 type sequence E description BINDING SITE FOR RESIDUE CL A 234 source : AC3 8) chain B residue 67 type sequence P description BINDING SITE FOR RESIDUE CL B 232 source : AC4 9) chain B residue 68 type sequence N description BINDING SITE FOR RESIDUE CL B 232 source : AC4 10) chain B residue 107 type sequence G description BINDING SITE FOR RESIDUE CL B 233 source : AC5 11) chain B residue 108 type sequence K description BINDING SITE FOR RESIDUE CL B 233 source : AC5 12) chain B residue 128 type sequence Q description BINDING SITE FOR RESIDUE CL B 233 source : AC5 13) chain A residue 62 type ACT_SITE sequence K description Proton donor => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI1 14) chain B residue 62 type ACT_SITE sequence K description Proton donor => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 11 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 33 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 17) chain B residue 60 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 120 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 19) chain B residue 181 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 20) chain B residue 190 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 21) chain B residue 210 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 22) chain B residue 211 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 33 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 24) chain A residue 60 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 25) chain A residue 120 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 181 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 190 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 210 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 211 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 30) chain B residue 11 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 57-70 type prosite sequence VFLDLKFHDIPNTC description OMPDECASE Orotidine 5'-phosphate decarboxylase active site. VFlDlKfhDIPnTC source prosite : PS00156

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