eF-site ID 3qej-AB PDB Code 3qej Chain A, B click to enlarge Title S74E-dCK mutant in complex with UDP Classification TRANSFERASE Compound Deoxycytidine kinase Source Homo sapiens (Human) (DCK_HUMAN) Sequence A:  TRIKKISIEGNIAAGKSTFVNILKQLSEDWEVVPEPVARW SNVELTMEQKNGGNVLQMMYEKPERWSFTFQTYACLSRIR AQLASLNGKLKDAEKPVLFFERSVYSDRYIFASNLYESES MNETEWTIYQDWHDWMNNQFGQSLELDGIIYLQATPETCL HRIYLRGRNEEQGIPLEYLEKLHYKHESWLLHRTLKTNFD YLQEVPILTLDVNEDFKDKYESLVEKVKEFLSTL B:  TRIKKISIEGNIAAGKSTFVNILKQLSEDWEVVPEPVARW SNVQLTMEQKNGGNVLQMMYEKPERWSFTFQTYACLSRIR AQLASLNGKLKDAEKPVLFFERSVYSDRYIFASNLYESES MNETEWTIYQDWHDWMNNQFGQSLELDGIIYLQATPETCL HRIYLRGRNEEQGIPLEYLEKLHYKHESWLLHRTLKTNFD YLQEVPILTLDVNEDFKDKYESLVEKVKEFLSTL Description Functional site 1) chain A residue 31 type sequence A description BINDING SITE FOR RESIDUE UDP A 401 source : AC1 2) chain A residue 32 type sequence A description BINDING SITE FOR RESIDUE UDP A 401 source : AC1 3) chain A residue 33 type sequence G description BINDING SITE FOR RESIDUE UDP A 401 source : AC1 4) chain A residue 34 type sequence K description BINDING SITE FOR RESIDUE UDP A 401 source : AC1 5) chain A residue 35 type sequence S description BINDING SITE FOR RESIDUE UDP A 401 source : AC1 6) chain A residue 36 type sequence T description BINDING SITE FOR RESIDUE UDP A 401 source : AC1 7) chain A residue 188 type sequence R description BINDING SITE FOR RESIDUE UDP A 401 source : AC1 8) chain A residue 192 type sequence R description BINDING SITE FOR RESIDUE UDP A 401 source : AC1 9) chain A residue 241 type sequence D description BINDING SITE FOR RESIDUE UDP A 401 source : AC1 10) chain A residue 242 type sequence F description BINDING SITE FOR RESIDUE UDP A 401 source : AC1 11) chain A residue 243 type sequence K description BINDING SITE FOR RESIDUE UDP A 401 source : AC1 12) chain B residue 29 type sequence N description BINDING SITE FOR RESIDUE UDP B 402 source : AC2 13) chain B residue 31 type sequence A description BINDING SITE FOR RESIDUE UDP B 402 source : AC2 14) chain B residue 32 type sequence A description BINDING SITE FOR RESIDUE UDP B 402 source : AC2 15) chain B residue 33 type sequence G description BINDING SITE FOR RESIDUE UDP B 402 source : AC2 16) chain B residue 34 type sequence K description BINDING SITE FOR RESIDUE UDP B 402 source : AC2 17) chain B residue 35 type sequence S description BINDING SITE FOR RESIDUE UDP B 402 source : AC2 18) chain B residue 36 type sequence T description BINDING SITE FOR RESIDUE UDP B 402 source : AC2 19) chain B residue 188 type sequence R description BINDING SITE FOR RESIDUE UDP B 402 source : AC2 20) chain B residue 192 type sequence R description BINDING SITE FOR RESIDUE UDP B 402 source : AC2 21) chain B residue 241 type sequence D description BINDING SITE FOR RESIDUE UDP B 402 source : AC2 22) chain B residue 242 type sequence F description BINDING SITE FOR RESIDUE UDP B 402 source : AC2 23) chain B residue 243 type sequence K description BINDING SITE FOR RESIDUE UDP B 402 source : AC2 24) chain B residue 28 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 25) chain B residue 53 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 26) chain B residue 86 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 27) chain B residue 97 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI2 28) chain B residue 128 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 29) chain B residue 133 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 30) chain B residue 188 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 31) chain B residue 197 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 32) chain B residue 240 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 33) chain A residue 86 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 34) chain A residue 97 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI2 35) chain A residue 128 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 36) chain A residue 133 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 37) chain A residue 188 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 38) chain A residue 197 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 39) chain A residue 240 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 40) chain A residue 28 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 41) chain A residue 53 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 42) chain A residue 72 type MOD_RES sequence T description Phosphothreonine; by CK1 => ECO:0000305|PubMed:20637175 source Swiss-Prot : SWS_FT_FI4 43) chain B residue 72 type MOD_RES sequence T description Phosphothreonine; by CK1 => ECO:0000305|PubMed:20637175 source Swiss-Prot : SWS_FT_FI4 44) chain A residue 74 type MOD_RES sequence E description Phosphoserine => ECO:0000269|PubMed:20637175, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 45) chain B residue 74 type MOD_RES sequence E description Phosphoserine => ECO:0000269|PubMed:20637175, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 46) chain A residue 127 type ACT_SITE sequence E description Proton acceptor => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 47) chain B residue 127 type ACT_SITE sequence E description Proton acceptor => ECO:0000255 source Swiss-Prot : SWS_FT_FI1

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