eF-site ID 6i2p-A PDB Code 6i2p Chain A click to enlarge Title Crystal structure of the Mycobacterium tuberculosis PknB kinase domain (L33E mutant) in complex with its substrate GarA Classification SIGNALING PROTEIN Compound Serine/threonine-protein kinase PknB Source (6I2P) Sequence A:  MTTPSHLSDRYELGEILGFGGMSEVHLARDLREHRDVAVK VLRADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEA ETPAGPLPYIVMEYVDGVTLRDIVHTEGPMTPKRAIEVIA DACQALNFSHQNGIIHRDVKPANIMISATNAVKVMDFGIA RNSVXQXAAVIGTAQYLSPEQARGDSVDARSDVYSLGCVL YEVLTGEPPFTGDSPVSVAYQHVREDPIPPSARHEGLSAD LDAVVLKALAKNPENRYQTAAEMRADLVRVHN Description Functional site 1) chain A residue 19 type sequence F description binding site for residue ACP A 301 source : AC1 2) chain A residue 20 type sequence G description binding site for residue ACP A 301 source : AC1 3) chain A residue 21 type sequence G description binding site for residue ACP A 301 source : AC1 4) chain A residue 23 type sequence S description binding site for residue ACP A 301 source : AC1 5) chain A residue 25 type sequence V description binding site for residue ACP A 301 source : AC1 6) chain A residue 38 type sequence A description binding site for residue ACP A 301 source : AC1 7) chain A residue 40 type sequence K description binding site for residue ACP A 301 source : AC1 8) chain A residue 72 type sequence V description binding site for residue ACP A 301 source : AC1 9) chain A residue 93 type sequence E description binding site for residue ACP A 301 source : AC1 10) chain A residue 95 type sequence V description binding site for residue ACP A 301 source : AC1 11) chain A residue 99 type sequence T description binding site for residue ACP A 301 source : AC1 12) chain A residue 145 type sequence M description binding site for residue ACP A 301 source : AC1 13) chain A residue 155 type sequence M description binding site for residue ACP A 301 source : AC1 14) chain A residue 59 type sequence E description binding site for residue MG A 302 source : AC2 15) chain A residue 156 type sequence D description binding site for residue MG A 302 source : AC2 16) chain A residue 29 type sequence R description binding site for residue SO4 A 303 source : AC3 17) chain A residue 30 type sequence D description binding site for residue SO4 A 303 source : AC3 18) chain A residue 31 type sequence L description binding site for residue SO4 A 303 source : AC3 19) chain A residue 34 type sequence H description binding site for residue SO4 A 303 source : AC3 20) chain A residue 137 type sequence R description binding site for residue SO4 D 202 source : AC7 21) chain A residue 93 type MOD_RES sequence E description Phosphothreonine; by PknG => ECO:0000269|PubMed:19019160 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 140 type MOD_RES sequence K description Phosphothreonine; by PknG => ECO:0000269|PubMed:19019160 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 17-40 type prosite sequence LGFGGMSEVHLARDLREHRDVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGFGGMSEVHlArdlrehrd..........VAVK source prosite : PS00107 24) chain A residue 134-146 type prosite sequence IIHRDVKPANIMI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDVKpaNIMI source prosite : PS00108 25) chain A residue 2 type MOD_RES sequence T description N-acetylthreonine => ECO:0007744|PubMed:21969609 source Swiss-Prot : SWS_FT_FI4 26) chain A residue 169 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000269|PubMed:12548283 source Swiss-Prot : SWS_FT_FI6 27) chain A residue 171 type MOD_RES sequence X description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:12950916, ECO:0000269|PubMed:15967413, ECO:0000269|PubMed:15985609, ECO:0000269|PubMed:19008858 source Swiss-Prot : SWS_FT_FI7 28) chain A residue 173 type MOD_RES sequence X description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:12950916, ECO:0000269|PubMed:15967413, ECO:0000269|PubMed:15985609 source Swiss-Prot : SWS_FT_FI8

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