eF-site ID 2h34-AB PDB Code 2h34 Chain A, B click to enlarge Title Apoenzyme crystal structure of the tuberculosis serine/threonine kinase, PknE Classification TRANSFERASE Compound Serine/threonine-protein kinase pknE Source (PKNE_MYCTU) Sequence A:  GPYRLRRLVGRGGXGDVYEAEDTVRERIVALKLXSETLSS DPVFRTRXQREARTAGRLQEPHVVPIHDFGEIDGQLYVDX RLINGVDLAAXLRRQGPLAPPRAVAIVRQIGSALDAAHAA GATHRDVKPENILVSADDFAYLVDFGIGTLYYXAPERFSE YRADIYALTCVLYECLTGSPPYQGDQLSVXGAHINQAIPR PSTVRPGIPVAFDAVIARGXAKNPEDRYVTCGDLSAAAHA ALA B:  GPYRLRRLVGRGGXGDVYEAEDTVRERIVALKLXSETLSS DPVFRTRXQREARTAGRLQEPHVVPIHDFGEIDGQLYVDX RLINGVDLAAXLRRQGPLAPPRAVAIVRQIGSALDAAHAA GATHRDVKPENILVSADDFAYLVDFGIGTLYYXAPERFSE YRADIYALTCVLYECLTGSPPYQGDQLSVXGAHINQAIPR PSTVRPGIPVAFDAVIARGXAKNPEDRYVTCGDLSAAAHA ALA Description (1)  Apoenzyme crystal structure of the Tuberculosis serine/threonine kinase, PknE Functional site 1) chain B residue 128 type sequence D description BINDING SITE FOR RESIDUE NA B 290 source : AC1 2) chain B residue 131 type sequence H description BINDING SITE FOR RESIDUE NA B 290 source : AC1 3) chain B residue 197 type sequence D description BINDING SITE FOR RESIDUE NA B 290 source : AC1 4) chain A residue 197 type sequence D description BINDING SITE FOR RESIDUE NA A 301 source : AC2 5) chain A residue 198 type sequence I description BINDING SITE FOR RESIDUE NA A 301 source : AC2 6) chain A residue 139 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI1 7) chain B residue 139 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI1 8) chain A residue 22 type BINDING sequence V description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 9) chain A residue 45 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 10) chain B residue 22 type BINDING sequence V description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 11) chain B residue 45 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 12) chain B residue 178 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:15967413 source Swiss-Prot : SWS_FT_FI4 13) chain A residue 50 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:15967413 source Swiss-Prot : SWS_FT_FI4 14) chain A residue 59 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:15967413 source Swiss-Prot : SWS_FT_FI4 15) chain A residue 178 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:15967413 source Swiss-Prot : SWS_FT_FI4 16) chain B residue 50 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:15967413 source Swiss-Prot : SWS_FT_FI4 17) chain B residue 59 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:15967413 source Swiss-Prot : SWS_FT_FI4 18) chain A residue 22-45 type prosite sequence VGRGGXGDVYEAEDTVRERIVALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGRGGMGDVYeAedtvreri..........VALK source prosite : PS00107

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