eF-site ID 2hve-ABC PDB Code 2hve Chain A, B, C click to enlarge Title S120G mutant of human nucleoside diphosphate kinase A complexed with ADP Classification SIGNALING PROTEIN,TRANSFERASE Compound Nucleoside diphosphate kinase A Source Homo sapiens (Human) (NDKA_HUMAN) Sequence A:  ANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFM QASEDLLKEHYVDLKDRPFFAGLVKYMHSGPVVAMVWEGL NVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGGD SVESAEKEIGLWFHPEELVDYTSCAQNWIYE B:  ANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFM QASEDLLKEHYVDLKDRPFFAGLVKYMHSGPVVAMVWEGL NVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGGD SVESAEKEIGLWFHPEELVDYTSCAQNWIYE C:  ANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFM QASEDLLKEHYVDLKDRPFFAGLVKYMHSGPVVAMVWEGL NVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGGD SVESAEKEIGLWFHPEELVDYTSCAQNWIYE Description Functional site 1) chain A residue 12 type sequence K description BINDING SITE FOR RESIDUE ADP A 160 source : AC1 2) chain A residue 52 type sequence Y description BINDING SITE FOR RESIDUE ADP A 160 source : AC1 3) chain A residue 55 type sequence L description BINDING SITE FOR RESIDUE ADP A 160 source : AC1 4) chain A residue 60 type sequence F description BINDING SITE FOR RESIDUE ADP A 160 source : AC1 5) chain A residue 64 type sequence L description BINDING SITE FOR RESIDUE ADP A 160 source : AC1 6) chain A residue 88 type sequence R description BINDING SITE FOR RESIDUE ADP A 160 source : AC1 7) chain A residue 94 type sequence T description BINDING SITE FOR RESIDUE ADP A 160 source : AC1 8) chain A residue 112 type sequence V description BINDING SITE FOR RESIDUE ADP A 160 source : AC1 9) chain A residue 115 type sequence N description BINDING SITE FOR RESIDUE ADP A 160 source : AC1 10) chain B residue 12 type sequence K description BINDING SITE FOR RESIDUE ADP B 160 source : AC2 11) chain B residue 55 type sequence L description BINDING SITE FOR RESIDUE ADP B 160 source : AC2 12) chain B residue 60 type sequence F description BINDING SITE FOR RESIDUE ADP B 160 source : AC2 13) chain B residue 64 type sequence L description BINDING SITE FOR RESIDUE ADP B 160 source : AC2 14) chain B residue 88 type sequence R description BINDING SITE FOR RESIDUE ADP B 160 source : AC2 15) chain B residue 94 type sequence T description BINDING SITE FOR RESIDUE ADP B 160 source : AC2 16) chain B residue 112 type sequence V description BINDING SITE FOR RESIDUE ADP B 160 source : AC2 17) chain B residue 115 type sequence N description BINDING SITE FOR RESIDUE ADP B 160 source : AC2 18) chain C residue 12 type sequence K description BINDING SITE FOR RESIDUE ADP C 160 source : AC3 19) chain C residue 55 type sequence L description BINDING SITE FOR RESIDUE ADP C 160 source : AC3 20) chain C residue 60 type sequence F description BINDING SITE FOR RESIDUE ADP C 160 source : AC3 21) chain C residue 88 type sequence R description BINDING SITE FOR RESIDUE ADP C 160 source : AC3 22) chain C residue 94 type sequence T description BINDING SITE FOR RESIDUE ADP C 160 source : AC3 23) chain C residue 112 type sequence V description BINDING SITE FOR RESIDUE ADP C 160 source : AC3 24) chain C residue 115 type sequence N description BINDING SITE FOR RESIDUE ADP C 160 source : AC3 25) chain A residue 118 type ACT_SITE sequence H description Pros-phosphohistidine intermediate => ECO:0000269|PubMed:1851158 source Swiss-Prot : SWS_FT_FI1 26) chain B residue 118 type ACT_SITE sequence H description Pros-phosphohistidine intermediate => ECO:0000269|PubMed:1851158 source Swiss-Prot : SWS_FT_FI1 27) chain C residue 118 type ACT_SITE sequence H description Pros-phosphohistidine intermediate => ECO:0000269|PubMed:1851158 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 12 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 29) chain B residue 94 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 30) chain B residue 105 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 31) chain B residue 115 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 32) chain C residue 12 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 33) chain C residue 60 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 34) chain C residue 88 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 35) chain C residue 94 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 36) chain C residue 105 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 37) chain C residue 115 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 38) chain A residue 60 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 39) chain A residue 88 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 40) chain A residue 94 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 41) chain A residue 105 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 42) chain A residue 115 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 43) chain B residue 12 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 44) chain B residue 60 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 45) chain B residue 88 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 46) chain A residue 120 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 47) chain A residue 122 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 48) chain A residue 125 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 49) chain B residue 120 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 50) chain B residue 122 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 51) chain B residue 125 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 52) chain C residue 120 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 53) chain C residue 122 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 54) chain C residue 125 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 55) chain A residue 100 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) source Swiss-Prot : SWS_FT_FI4 56) chain B residue 100 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) source Swiss-Prot : SWS_FT_FI4 57) chain C residue 100 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) source Swiss-Prot : SWS_FT_FI4

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