eF-site ID 2hur-ABCDEF PDB Code 2hur Chain A, B, C, D, E, F click to enlarge Title Escherichia coli nucleoside diphosphate kinase Classification SIGNALING PROTEIN,TRANSFERASE Compound NUCLEOSIDE DIPHOSPHATE KINASE Source Escherichia coli (strain K12) (NDK_ECOLI) Sequence A:  AIERTFSIIKPNAVAKNVIGNIFARFEAAGFKIVGTKMLH LTVEQARGFYAEHDGKPFFDGLVEFMTSGPIVVSVLEGEN AVQRHRDLLGATNPANALAGTLRADYADSLTENGTHGSDS VESAAREIAYFFGEGEVCPRTR B:  AIERTFSIIKPNAVAKNVIGNIFARFEAAGFKIVGTKMLH LTVEQARGFYAEHDGKPFFDGLVEFMTSGPIVVSVLEGEN AVQRHRDLLGATNPANALAGTLRADYADSLTENGTHGSDS VESAAREIAYFFGEGEVCPRTR C:  AIERTFSIIKPNAVAKNVIGNIFARFEAAGFKIVGTKMLH LTVEQARGFYAEHDGKPFFDGLVEFMTSGPIVVSVLEGEN AVQRHRDLLGATNPANALAGTLRADYADSLTENGTHGSDS VESAAREIAYFFGEGEVCPRTR D:  AIERTFSIIKPNAVAKNVIGNIFARFEAAGFKIVGTKMLH LTVEQARGFYAEHDGKPFFDGLVEFMTSGPIVVSVLEGEN AVQRHRDLLGATNPANALAGTLRADYADSLTENGTHGSDS VESAAREIAYFFGEGEVCPRTR E:  AIERTFSIIKPNAVAKNVIGNIFARFEAAGFKIVGTKMLH LTVEQARGFYAEHDGKPFFDGLVEFMTSGPIVVSVLEGEN AVQRHRDLLGATNPANALAGTLRADYADSLTENGTHGSDS VESAAREIAYFFGEGEVCPRTR F:  AIERTFSIIKPNAVAKNVIGNIFARFEAAGFKIVGTKMLH LTVEQARGFYAEHDGKPFFDGLVEFMTSGPIVVSVLEGEN AVQRHRDLLGATNPANALAGTLRADYADSLTENGTHGSDS VESAAREIAYFFGEGEVCPRTR Description Functional site 1) chain A residue 11 type sequence K description BINDING SITE FOR RESIDUE SO4 A 200 source : AC1 2) chain A residue 93 type sequence T description BINDING SITE FOR RESIDUE SO4 A 200 source : AC1 3) chain A residue 104 type sequence R description BINDING SITE FOR RESIDUE SO4 A 200 source : AC1 4) chain A residue 114 type sequence N description BINDING SITE FOR RESIDUE SO4 A 200 source : AC1 5) chain A residue 117 type sequence H description BINDING SITE FOR RESIDUE SO4 A 200 source : AC1 6) chain B residue 11 type sequence K description BINDING SITE FOR RESIDUE SO4 B 200 source : AC2 7) chain B residue 93 type sequence T description BINDING SITE FOR RESIDUE SO4 B 200 source : AC2 8) chain B residue 104 type sequence R description BINDING SITE FOR RESIDUE SO4 B 200 source : AC2 9) chain B residue 114 type sequence N description BINDING SITE FOR RESIDUE SO4 B 200 source : AC2 10) chain B residue 117 type sequence H description BINDING SITE FOR RESIDUE SO4 B 200 source : AC2 11) chain C residue 11 type sequence K description BINDING SITE FOR RESIDUE SO4 C 200 source : AC3 12) chain C residue 93 type sequence T description BINDING SITE FOR RESIDUE SO4 C 200 source : AC3 13) chain C residue 104 type sequence R description BINDING SITE FOR RESIDUE SO4 C 200 source : AC3 14) chain C residue 114 type sequence N description BINDING SITE FOR RESIDUE SO4 C 200 source : AC3 15) chain C residue 117 type sequence H description BINDING SITE FOR RESIDUE SO4 C 200 source : AC3 16) chain D residue 11 type sequence K description BINDING SITE FOR RESIDUE SO4 D 200 source : AC4 17) chain D residue 93 type sequence T description BINDING SITE FOR RESIDUE SO4 D 200 source : AC4 18) chain D residue 104 type sequence R description BINDING SITE FOR RESIDUE SO4 D 200 source : AC4 19) chain D residue 114 type sequence N description BINDING SITE FOR RESIDUE SO4 D 200 source : AC4 20) chain D residue 117 type sequence H description BINDING SITE FOR RESIDUE SO4 D 200 source : AC4 21) chain E residue 11 type sequence K description BINDING SITE FOR RESIDUE SO4 E 200 source : AC5 22) chain E residue 93 type sequence T description BINDING SITE FOR RESIDUE SO4 E 200 source : AC5 23) chain E residue 104 type sequence R description BINDING SITE FOR RESIDUE SO4 E 200 source : AC5 24) chain E residue 114 type sequence N description BINDING SITE FOR RESIDUE SO4 E 200 source : AC5 25) chain E residue 117 type sequence H description BINDING SITE FOR RESIDUE SO4 E 200 source : AC5 26) chain F residue 11 type sequence K description BINDING SITE FOR RESIDUE SO4 F 200 source : AC6 27) chain F residue 93 type sequence T description BINDING SITE FOR RESIDUE SO4 F 200 source : AC6 28) chain F residue 104 type sequence R description BINDING SITE FOR RESIDUE SO4 F 200 source : AC6 29) chain F residue 114 type sequence N description BINDING SITE FOR RESIDUE SO4 F 200 source : AC6 30) chain F residue 117 type sequence H description BINDING SITE FOR RESIDUE SO4 F 200 source : AC6 31) chain A residue 12 type BINDING sequence P description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 32) chain B residue 94 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 33) chain B residue 105 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 34) chain B residue 115 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 35) chain C residue 12 type BINDING sequence P description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 36) chain C residue 60 type BINDING sequence F description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 37) chain C residue 88 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 38) chain C residue 94 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 39) chain C residue 105 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 40) chain C residue 115 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 41) chain D residue 12 type BINDING sequence P description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 42) chain A residue 60 type BINDING sequence F description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 43) chain D residue 60 type BINDING sequence F description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 44) chain D residue 88 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 45) chain D residue 94 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 46) chain D residue 105 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 47) chain D residue 115 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 48) chain E residue 12 type BINDING sequence P description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 49) chain E residue 60 type BINDING sequence F description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 50) chain E residue 88 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 51) chain E residue 94 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 52) chain E residue 105 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 53) chain A residue 88 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 54) chain E residue 115 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 55) chain F residue 12 type BINDING sequence P description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 56) chain F residue 60 type BINDING sequence F description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 57) chain F residue 88 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 58) chain F residue 94 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 59) chain F residue 105 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 60) chain F residue 115 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 61) chain A residue 94 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 62) chain A residue 105 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 63) chain A residue 115 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 64) chain B residue 12 type BINDING sequence P description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 65) chain B residue 60 type BINDING sequence F description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 66) chain B residue 88 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI2 67) chain A residue 118 type ACT_SITE sequence G description Pros-phosphohistidine intermediate => ECO:0000250|UniProtKB:P15531, ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI1 68) chain B residue 118 type ACT_SITE sequence G description Pros-phosphohistidine intermediate => ECO:0000250|UniProtKB:P15531, ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI1 69) chain C residue 118 type ACT_SITE sequence G description Pros-phosphohistidine intermediate => ECO:0000250|UniProtKB:P15531, ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI1 70) chain D residue 118 type ACT_SITE sequence G description Pros-phosphohistidine intermediate => ECO:0000250|UniProtKB:P15531, ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI1 71) chain E residue 118 type ACT_SITE sequence G description Pros-phosphohistidine intermediate => ECO:0000250|UniProtKB:P15531, ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI1 72) chain F residue 118 type ACT_SITE sequence G description Pros-phosphohistidine intermediate => ECO:0000250|UniProtKB:P15531, ECO:0000255|HAMAP-Rule:MF_00451 source Swiss-Prot : SWS_FT_FI1 73) chain A residue 120 type MOD_RES sequence D description Phosphoserine => ECO:0000269|PubMed:7730286 source Swiss-Prot : SWS_FT_FI3 74) chain E residue 122 type MOD_RES sequence V description Phosphoserine => ECO:0000269|PubMed:7730286 source Swiss-Prot : SWS_FT_FI3 75) chain F residue 120 type MOD_RES sequence D description Phosphoserine => ECO:0000269|PubMed:7730286 source Swiss-Prot : SWS_FT_FI3 76) chain F residue 122 type MOD_RES sequence V description Phosphoserine => ECO:0000269|PubMed:7730286 source Swiss-Prot : SWS_FT_FI3 77) chain A residue 122 type MOD_RES sequence V description Phosphoserine => ECO:0000269|PubMed:7730286 source Swiss-Prot : SWS_FT_FI3 78) chain B residue 120 type MOD_RES sequence D description Phosphoserine => ECO:0000269|PubMed:7730286 source Swiss-Prot : SWS_FT_FI3 79) chain B residue 122 type MOD_RES sequence V description Phosphoserine => ECO:0000269|PubMed:7730286 source Swiss-Prot : SWS_FT_FI3 80) chain C residue 120 type MOD_RES sequence D description Phosphoserine => ECO:0000269|PubMed:7730286 source Swiss-Prot : SWS_FT_FI3 81) chain C residue 122 type MOD_RES sequence V description Phosphoserine => ECO:0000269|PubMed:7730286 source Swiss-Prot : SWS_FT_FI3 82) chain D residue 120 type MOD_RES sequence D description Phosphoserine => ECO:0000269|PubMed:7730286 source Swiss-Prot : SWS_FT_FI3 83) chain D residue 122 type MOD_RES sequence V description Phosphoserine => ECO:0000269|PubMed:7730286 source Swiss-Prot : SWS_FT_FI3 84) chain E residue 120 type MOD_RES sequence D description Phosphoserine => ECO:0000269|PubMed:7730286 source Swiss-Prot : SWS_FT_FI3 85) chain A residue 114-122 type prosite sequence NGTHGSDSV description NDPK Nucleoside diphosphate kinase (NDPK) active site signature. NgtHGSDSV source prosite : PS00469

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