eF-site ID 4o0t-A PDB Code 4o0t Chain A click to enlarge Title Back pocket flexibility provides group-II PAK selectivity for type 1 kinase inhibitors Classification transferase/transferase inhibitor Compound Serine/threonine-protein kinase PAK 1 Source Homo sapiens (Human) (PAK1_HUMAN) Sequence A:  EEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDV ATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNY LDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVC RECLQALEFLHSNQVIHRNIKSDNILLGMDGSVKLTDFGF CAQITPEQSKRSEMVGTPYWMAPEVVTRKAYGPKVDIWSL GIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKL SAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSL TPLIAAAKEATK Description Functional site 1) chain A residue 276 type sequence I description BINDING SITE FOR RESIDUE 2OL A 601 source : AC1 2) chain A residue 284 type sequence V description BINDING SITE FOR RESIDUE 2OL A 601 source : AC1 3) chain A residue 299 type sequence K description BINDING SITE FOR RESIDUE 2OL A 601 source : AC1 4) chain A residue 315 type sequence E description BINDING SITE FOR RESIDUE 2OL A 601 source : AC1 5) chain A residue 319 type sequence M description BINDING SITE FOR RESIDUE 2OL A 601 source : AC1 6) chain A residue 328 type sequence V description BINDING SITE FOR RESIDUE 2OL A 601 source : AC1 7) chain A residue 344 type sequence M description BINDING SITE FOR RESIDUE 2OL A 601 source : AC1 8) chain A residue 345 type sequence E description BINDING SITE FOR RESIDUE 2OL A 601 source : AC1 9) chain A residue 346 type sequence Y description BINDING SITE FOR RESIDUE 2OL A 601 source : AC1 10) chain A residue 347 type sequence L description BINDING SITE FOR RESIDUE 2OL A 601 source : AC1 11) chain A residue 351 type sequence S description BINDING SITE FOR RESIDUE 2OL A 601 source : AC1 12) chain A residue 406 type sequence T description BINDING SITE FOR RESIDUE 2OL A 601 source : AC1 13) chain A residue 407 type sequence D description BINDING SITE FOR RESIDUE 2OL A 601 source : AC1 14) chain A residue 408 type sequence F description BINDING SITE FOR RESIDUE 2OL A 601 source : AC1 15) chain A residue 285 type MOD_RES sequence Y description Phosphotyrosine; by JAK2 => ECO:0000269|PubMed:17726028, ECO:0000269|PubMed:17989089 source Swiss-Prot : SWS_FT_FI3 16) chain A residue 423 type MOD_RES sequence E description Phosphothreonine; by autocatalysis, BRSK2 and PDPK1 => ECO:0000269|PubMed:10551809, ECO:0000269|PubMed:10995762, ECO:0000269|PubMed:22153498, ECO:0000269|PubMed:22669945 source Swiss-Prot : SWS_FT_FI4 17) chain A residue 389 type ACT_SITE sequence N description Proton acceptor => ECO:0000269|PubMed:22153498 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 276 type BINDING sequence I description BINDING => ECO:0000269|PubMed:22153498 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 299 type BINDING sequence K description BINDING => ECO:0000269|PubMed:22153498 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 345 type BINDING sequence E description BINDING => ECO:0000269|PubMed:22153498 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 276-299 type prosite sequence IGQGASGTVYTAMDVATGQEVAIK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGQGASGTVYtAmdvatgqe..........VAIK source prosite : PS00107

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