eF-site ID 3fbb-BDF PDB Code 3fbb Chain B, D, F click to enlarge Title Crystal structure of the Mimivirus NDK N62L-R107G double mutant complexed with UDP Classification TRANSFERASE Compound Nucleoside diphosphate kinase Source null (NDK_MIMIV) Sequence B:  LQRTLVLIKPDAFERSLVAEIMGRIEKKNFKIVSMKFWSK APRNLIEQHYKEHSEQSYFNDLCDFMVSGPIISIVYEGTD AISKIRRLQGNILTPGTIRGDLANDIGENLIHASDSEDSA VDEISIWFPE D:  GLQRTLVLIKPDAFERSLVAEIMGRIEKKNFKIVSMKFWS KAPRNLIEQHYKEHSEQSYFNDLCDFMVSGPIISIVYEGT DAISKIRRLQGNILTPGTIRGDLANDIGENLIHASDSEDS AVDEISIWFPET F:  GLQRTLVLIKPDAFERSLVAEIMGRIEKKNFKIVSMKFWS KAPRNLIEQHYKEHSEQSYFNDLCDFMVSGPIISIVYEGT DAISKIRRLQGNILTPGTIRGDLANDIGENLIHASDSEDS AVDEISIWFP Description Functional site 1) chain B residue 9 type sequence K description BINDING SITE FOR RESIDUE UDP B 201 source : AC4 2) chain B residue 50 type sequence Y description BINDING SITE FOR RESIDUE UDP B 201 source : AC4 3) chain B residue 53 type sequence H description BINDING SITE FOR RESIDUE UDP B 201 source : AC4 4) chain B residue 58 type sequence Y description BINDING SITE FOR RESIDUE UDP B 201 source : AC4 5) chain B residue 62 type sequence L description BINDING SITE FOR RESIDUE UDP B 201 source : AC4 6) chain B residue 86 type sequence R description BINDING SITE FOR RESIDUE UDP B 201 source : AC4 7) chain B residue 99 type sequence R description BINDING SITE FOR RESIDUE UDP B 201 source : AC4 8) chain B residue 106 type sequence I description BINDING SITE FOR RESIDUE UDP B 201 source : AC4 9) chain B residue 107 type sequence G description BINDING SITE FOR RESIDUE UDP B 201 source : AC4 10) chain B residue 109 type sequence N description BINDING SITE FOR RESIDUE UDP B 201 source : AC4 11) chain D residue 115 type sequence D description BINDING SITE FOR RESIDUE MG D 202 source : AC7 12) chain D residue 9 type sequence K description BINDING SITE FOR RESIDUE UDP D 201 source : AC8 13) chain D residue 53 type sequence H description BINDING SITE FOR RESIDUE UDP D 201 source : AC8 14) chain D residue 58 type sequence Y description BINDING SITE FOR RESIDUE UDP D 201 source : AC8 15) chain D residue 62 type sequence L description BINDING SITE FOR RESIDUE UDP D 201 source : AC8 16) chain D residue 86 type sequence R description BINDING SITE FOR RESIDUE UDP D 201 source : AC8 17) chain D residue 99 type sequence R description BINDING SITE FOR RESIDUE UDP D 201 source : AC8 18) chain D residue 106 type sequence I description BINDING SITE FOR RESIDUE UDP D 201 source : AC8 19) chain D residue 107 type sequence G description BINDING SITE FOR RESIDUE UDP D 201 source : AC8 20) chain D residue 109 type sequence N description BINDING SITE FOR RESIDUE UDP D 201 source : AC8 21) chain F residue 86 type sequence R description BINDING SITE FOR RESIDUE MG F 202 source : BC2 22) chain F residue 115 type sequence D description BINDING SITE FOR RESIDUE MG F 202 source : BC2 23) chain F residue 9 type sequence K description BINDING SITE FOR RESIDUE UDP F 201 source : BC3 24) chain F residue 53 type sequence H description BINDING SITE FOR RESIDUE UDP F 201 source : BC3 25) chain F residue 62 type sequence L description BINDING SITE FOR RESIDUE UDP F 201 source : BC3 26) chain F residue 86 type sequence R description BINDING SITE FOR RESIDUE UDP F 201 source : BC3 27) chain F residue 99 type sequence R description BINDING SITE FOR RESIDUE UDP F 201 source : BC3 28) chain F residue 106 type sequence I description BINDING SITE FOR RESIDUE UDP F 201 source : BC3 29) chain F residue 107 type sequence G description BINDING SITE FOR RESIDUE UDP F 201 source : BC3 30) chain F residue 109 type sequence N description BINDING SITE FOR RESIDUE UDP F 201 source : BC3 31) chain B residue 112 type ACT_SITE sequence H description Pros-phosphohistidine intermediate => ECO:0000255|PROSITE-ProRule:PRU10030 source Swiss-Prot : SWS_FT_FI1 32) chain D residue 112 type ACT_SITE sequence H description Pros-phosphohistidine intermediate => ECO:0000255|PROSITE-ProRule:PRU10030 source Swiss-Prot : SWS_FT_FI1 33) chain F residue 112 type ACT_SITE sequence H description Pros-phosphohistidine intermediate => ECO:0000255|PROSITE-ProRule:PRU10030 source Swiss-Prot : SWS_FT_FI1 34) chain B residue 9 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 35) chain B residue 58 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 36) chain B residue 86 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 37) chain B residue 99 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 38) chain B residue 109 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 39) chain D residue 9 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 40) chain D residue 58 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 41) chain D residue 86 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 42) chain D residue 99 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 43) chain D residue 109 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 44) chain F residue 9 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 45) chain F residue 58 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 46) chain F residue 86 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 47) chain F residue 99 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 48) chain F residue 109 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2

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