eF-site ID 5m57-A PDB Code 5m57 Chain A click to enlarge Title Nek2 bound to arylaminopurine 6 Classification TRANSFERASE Compound Serine/threonine-protein kinase Nek2 Source Homo sapiens (Human) (NEK2_HUMAN) Sequence A:  SRAEDYEVLYTIGTGSYGRCQKIRRKSDGKILVWKELDYG SMTEAEKQMLVSEVNLLRELKHPNIVRYYDRIIDRTNTTL YIVMEYCEGGDLASVITKGTKERQYLDEEFVLRVMTQLTL ALKECHRRSDGGHTVLHRDLKPANVFLDGKQNVKLGDFVG TPYYMSPEQMNRMSYNEKSDIWSLGCLLYELCALMPPFTA FSQKELAGKIREGKFRRIPYRYSDELNEIITRMLNLKDYH RPSVEEILENPLILEHHHHHH Description Functional site 1) chain A residue 17 type sequence G description binding site for residue 4SP A 301 source : AC1 2) chain A residue 19 type sequence Y description binding site for residue 4SP A 301 source : AC1 3) chain A residue 22 type sequence C description binding site for residue 4SP A 301 source : AC1 4) chain A residue 37 type sequence K description binding site for residue 4SP A 301 source : AC1 5) chain A residue 87 type sequence E description binding site for residue 4SP A 301 source : AC1 6) chain A residue 89 type sequence C description binding site for residue 4SP A 301 source : AC1 7) chain A residue 92 type sequence G description binding site for residue 4SP A 301 source : AC1 8) chain A residue 96 type sequence S description binding site for residue 4SP A 301 source : AC1 9) chain A residue 148 type sequence F description binding site for residue 4SP A 301 source : AC1 10) chain A residue 159 type sequence D description binding site for residue 4SP A 301 source : AC1 11) chain A residue 184 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 12) chain A residue 241 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000269|PubMed:17197699 source Swiss-Prot : SWS_FT_FI8 13) chain A residue 137-149 type prosite sequence VLHRDLKPANVFL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpaNVFL source prosite : PS00108 14) chain A residue 14 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 37 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 16) chain A residue 141 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 179 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:17197699 source Swiss-Prot : SWS_FT_FI6

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