eF-site ID 4tpt-AB PDB Code 4tpt Chain A, B click to enlarge Title Crystal Structure of the Human LIMK2 Kinase Domain In Complex With a Non-ATP Competitive Inhibitor Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound LIM domain kinase 2 Source Homo sapiens (Human) (LIMK2_HUMAN) Sequence A:  DLIHGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEET QKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIE GGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIH RDLNSHNCLIKLDKTVVVADFGLSRLIVKKRYTVVGNPYW MAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPR TLDFGLNVKLFWEKFVPTDCPPAFFPLAAICCRLEPESRP AFSKLEDSFEALSLYLGELGIPLPAELEELDHTVSMQYG B:  DLIHGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEET QKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIE GGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIH RDLNSHNCLIKLDKTVVVADFGLSRLIVYTVVGNPYWMAP EMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPRTLD FGLNVKLFWEKFVPTDCPPAFFPLAAICCRLEPESRPAFS KLEDSFEALSLYLGELGIPLPAELEELDHTVSMQYGL Description Functional site 1) chain A residue 361 type sequence E description binding site for residue 35H A 701 source : AC1 2) chain A residue 363 type sequence I description binding site for residue 35H A 701 source : AC1 3) chain A residue 380 type sequence M description binding site for residue 35H A 701 source : AC1 4) chain A residue 383 type sequence L description binding site for residue 35H A 701 source : AC1 5) chain A residue 388 type sequence V description binding site for residue 35H A 701 source : AC1 6) chain A residue 389 type sequence L description binding site for residue 35H A 701 source : AC1 7) chain A residue 391 type sequence F description binding site for residue 35H A 701 source : AC1 8) chain A residue 405 type sequence T description binding site for residue 35H A 701 source : AC1 9) chain A residue 467 type sequence V description binding site for residue 35H A 701 source : AC1 10) chain A residue 468 type sequence A description binding site for residue 35H A 701 source : AC1 11) chain A residue 469 type sequence D description binding site for residue 35H A 701 source : AC1 12) chain A residue 470 type sequence F description binding site for residue 35H A 701 source : AC1 13) chain A residue 472 type sequence L description binding site for residue 35H A 701 source : AC1 14) chain A residue 474 type sequence R description binding site for residue 35H A 701 source : AC1 15) chain B residue 360 type sequence K description binding site for residue 35H B 701 source : AC2 16) chain B residue 361 type sequence E description binding site for residue 35H B 701 source : AC2 17) chain B residue 362 type sequence L description binding site for residue 35H B 701 source : AC2 18) chain B residue 363 type sequence I description binding site for residue 35H B 701 source : AC2 19) chain B residue 380 type sequence M description binding site for residue 35H B 701 source : AC2 20) chain B residue 383 type sequence L description binding site for residue 35H B 701 source : AC2 21) chain B residue 388 type sequence V description binding site for residue 35H B 701 source : AC2 22) chain B residue 389 type sequence L description binding site for residue 35H B 701 source : AC2 23) chain B residue 391 type sequence F description binding site for residue 35H B 701 source : AC2 24) chain B residue 405 type sequence T description binding site for residue 35H B 701 source : AC2 25) chain B residue 449 type sequence H description binding site for residue 35H B 701 source : AC2 26) chain B residue 467 type sequence V description binding site for residue 35H B 701 source : AC2 27) chain B residue 469 type sequence D description binding site for residue 35H B 701 source : AC2 28) chain B residue 470 type sequence F description binding site for residue 35H B 701 source : AC2 29) chain B residue 472 type sequence L description binding site for residue 35H B 701 source : AC2 30) chain B residue 474 type sequence R description binding site for residue 35H B 701 source : AC2 31) chain A residue 451 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:22328514 source Swiss-Prot : SWS_FT_FI1 32) chain B residue 451 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:22328514 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 337 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 360 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 35) chain B residue 337 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 36) chain B residue 360 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 37) chain A residue 505 type MOD_RES sequence T description Phosphothreonine; by ROCK1 and CDC42BP => ECO:0000269|PubMed:11018042, ECO:0000269|PubMed:11340065 source Swiss-Prot : SWS_FT_FI3 38) chain B residue 505 type MOD_RES sequence T description Phosphothreonine; by ROCK1 and CDC42BP => ECO:0000269|PubMed:11018042, ECO:0000269|PubMed:11340065 source Swiss-Prot : SWS_FT_FI3 39) chain A residue 337-360 type prosite sequence LGKGFFGQAIKVTHKATGKVMVMK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGFFGQAIkVthkatgkv..........MVMK source prosite : PS00107

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