eF-site ID 1ny3-A PDB Code 1ny3 Chain A click to enlarge Title Crystal structure of ADP bound to MAP KAP kinase 2 Classification TRANSFERASE Compound MAP kinase-activated protein kinase 2 Source Homo sapiens (Human) (MAPK2_HUMAN) Sequence A:  FHVKSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQIFNKR TQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYE NLYAGRKCLLIVMECLDGGELFSRIQDTEREASEIMKSIG EAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFA KETTSHPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGY PPFYSGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKT EPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKED Description Functional site 1) chain A residue 70 type sequence L description BINDING SITE FOR RESIDUE ADP A 401 source : AC1 2) chain A residue 71 type sequence G description BINDING SITE FOR RESIDUE ADP A 401 source : AC1 3) chain A residue 72 type sequence L description BINDING SITE FOR RESIDUE ADP A 401 source : AC1 4) chain A residue 73 type sequence G description BINDING SITE FOR RESIDUE ADP A 401 source : AC1 5) chain A residue 74 type sequence I description BINDING SITE FOR RESIDUE ADP A 401 source : AC1 6) chain A residue 91 type sequence A description BINDING SITE FOR RESIDUE ADP A 401 source : AC1 7) chain A residue 93 type sequence K description BINDING SITE FOR RESIDUE ADP A 401 source : AC1 8) chain A residue 139 type sequence E description BINDING SITE FOR RESIDUE ADP A 401 source : AC1 9) chain A residue 141 type sequence L description BINDING SITE FOR RESIDUE ADP A 401 source : AC1 10) chain A residue 191 type sequence N description BINDING SITE FOR RESIDUE ADP A 401 source : AC1 11) chain A residue 207 type sequence D description BINDING SITE FOR RESIDUE ADP A 401 source : AC1 12) chain A residue 70-93 type prosite sequence LGLGINGKVLQIFNKRTQEKFALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGLGINGKVLqIfnkrtqek..........FALK source prosite : PS00107 13) chain A residue 182-194 type prosite sequence IAHRDVKPENLLY description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHrDVKpeNLLY source prosite : PS00108 14) chain A residue 186 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 15) chain A residue 70 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 93 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 139 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 18) chain A residue 328 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 19) chain A residue 334 type MOD_RES sequence T description Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:8846784, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9

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