eF-site ID 3fbb-ACE PDB Code 3fbb Chain A, C, E click to enlarge Title Crystal structure of the Mimivirus NDK N62L-R107G double mutant complexed with UDP Classification TRANSFERASE Compound Nucleoside diphosphate kinase Source Acanthamoeba polyphaga mimivirus (APMV) (NDK_MIMIV) Sequence A:  AGLQRTLVLIKPDAFERSLVAEIMGRIEKKNFKIVSMKFW SKAPRNLIEQHYKEHSEQSYFNDLCDFMVSGPIISIVYEG TDAISKIRRLQGNILTPGTIRGDLANDIGENLIHASDSED SAVDEISIWFPET C:  GLQRTLVLIKPDAFERSLVAEIMGRIEKKNFKIVSMKFWS KAPRNLIEQHYKEHSEQSYFNDLCDFMVSGPIISIVYEGT DAISKIRRLQGNILTPGTIRGDLANDIGENLIHASDSEDS AVDEISIWFPET E:  GLQRTLVLIKPDAFERSLVAEIMGRIEKKNFKIVSMKFWS KAPRNLIEQHYKEHSEQSYFNDLCDFMVSGPIISIVYEGT DAISKIRRLQGNILTPGTIRGDLANDIGENLIHASDSEDS AVDEISIWFPET Description Functional site 1) chain A residue 86 type sequence R description BINDING SITE FOR RESIDUE MG A 202 source : AC1 2) chain A residue 115 type sequence D description BINDING SITE FOR RESIDUE MG A 202 source : AC1 3) chain A residue 9 type sequence K description BINDING SITE FOR RESIDUE UDP A 201 source : AC2 4) chain A residue 53 type sequence H description BINDING SITE FOR RESIDUE UDP A 201 source : AC2 5) chain A residue 58 type sequence Y description BINDING SITE FOR RESIDUE UDP A 201 source : AC2 6) chain A residue 62 type sequence L description BINDING SITE FOR RESIDUE UDP A 201 source : AC2 7) chain A residue 86 type sequence R description BINDING SITE FOR RESIDUE UDP A 201 source : AC2 8) chain A residue 89 type sequence Q description BINDING SITE FOR RESIDUE UDP A 201 source : AC2 9) chain A residue 99 type sequence R description BINDING SITE FOR RESIDUE UDP A 201 source : AC2 10) chain A residue 106 type sequence I description BINDING SITE FOR RESIDUE UDP A 201 source : AC2 11) chain A residue 107 type sequence G description BINDING SITE FOR RESIDUE UDP A 201 source : AC2 12) chain A residue 109 type sequence N description BINDING SITE FOR RESIDUE UDP A 201 source : AC2 13) chain C residue 86 type sequence R description BINDING SITE FOR RESIDUE MG C 202 source : AC5 14) chain C residue 115 type sequence D description BINDING SITE FOR RESIDUE MG C 202 source : AC5 15) chain C residue 9 type sequence K description BINDING SITE FOR RESIDUE UDP C 201 source : AC6 16) chain C residue 53 type sequence H description BINDING SITE FOR RESIDUE UDP C 201 source : AC6 17) chain C residue 58 type sequence Y description BINDING SITE FOR RESIDUE UDP C 201 source : AC6 18) chain C residue 62 type sequence L description BINDING SITE FOR RESIDUE UDP C 201 source : AC6 19) chain C residue 86 type sequence R description BINDING SITE FOR RESIDUE UDP C 201 source : AC6 20) chain C residue 89 type sequence Q description BINDING SITE FOR RESIDUE UDP C 201 source : AC6 21) chain C residue 99 type sequence R description BINDING SITE FOR RESIDUE UDP C 201 source : AC6 22) chain C residue 106 type sequence I description BINDING SITE FOR RESIDUE UDP C 201 source : AC6 23) chain C residue 107 type sequence G description BINDING SITE FOR RESIDUE UDP C 201 source : AC6 24) chain C residue 109 type sequence N description BINDING SITE FOR RESIDUE UDP C 201 source : AC6 25) chain E residue 86 type sequence R description BINDING SITE FOR RESIDUE MG E 202 source : AC9 26) chain E residue 115 type sequence D description BINDING SITE FOR RESIDUE MG E 202 source : AC9 27) chain E residue 9 type sequence K description BINDING SITE FOR RESIDUE UDP E 201 source : BC1 28) chain E residue 53 type sequence H description BINDING SITE FOR RESIDUE UDP E 201 source : BC1 29) chain E residue 58 type sequence Y description BINDING SITE FOR RESIDUE UDP E 201 source : BC1 30) chain E residue 62 type sequence L description BINDING SITE FOR RESIDUE UDP E 201 source : BC1 31) chain E residue 86 type sequence R description BINDING SITE FOR RESIDUE UDP E 201 source : BC1 32) chain E residue 99 type sequence R description BINDING SITE FOR RESIDUE UDP E 201 source : BC1 33) chain E residue 106 type sequence I description BINDING SITE FOR RESIDUE UDP E 201 source : BC1 34) chain E residue 107 type sequence G description BINDING SITE FOR RESIDUE UDP E 201 source : BC1 35) chain E residue 109 type sequence N description BINDING SITE FOR RESIDUE UDP E 201 source : BC1 36) chain A residue 109-117 type prosite sequence NLIHASDSE description NDPK Nucleoside diphosphate kinase (NDPK) active site signature. NliHASDSE source prosite : PS00469 37) chain A residue 9 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 38) chain C residue 9 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 39) chain C residue 58 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 40) chain C residue 86 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 41) chain C residue 99 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 42) chain C residue 109 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 43) chain A residue 58 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 44) chain E residue 9 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 45) chain E residue 58 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 46) chain E residue 86 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 47) chain E residue 99 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 48) chain E residue 109 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 49) chain A residue 86 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 50) chain A residue 99 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 51) chain A residue 109 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 52) chain A residue 112 type ACT_SITE sequence H description Pros-phosphohistidine intermediate => ECO:0000255|PROSITE-ProRule:PRU10030 source Swiss-Prot : SWS_FT_FI1 53) chain C residue 112 type ACT_SITE sequence H description Pros-phosphohistidine intermediate => ECO:0000255|PROSITE-ProRule:PRU10030 source Swiss-Prot : SWS_FT_FI1 54) chain E residue 112 type ACT_SITE sequence H description Pros-phosphohistidine intermediate => ECO:0000255|PROSITE-ProRule:PRU10030 source Swiss-Prot : SWS_FT_FI1

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