eF-site ID 6i2p-B PDB Code 6i2p Chain B 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 B:  TTPSHLSDRYELGEILGFGGMSEVHLARDLREHRDVAVKV LRADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAE TPAGPLPYIVMEYVDGVTLRDIVHTEGPMTPKRAIEVIAD ACQALNFSHQNGIIHRDVKPANIMISATNAVKVMDFGIAN SVXQXAATAQYLSPEQARGDSVDARSDVYSLGCVLYEVLT GEPPFTGDSPVSVAYQHVREDPIPPSARHEGLSADLDAVV LKALAKNPENRYQTAAEMRADLVRVH Description Functional site 1) chain B residue 18 type sequence G description binding site for residue ACP B 301 source : AC4 2) chain B residue 19 type sequence F description binding site for residue ACP B 301 source : AC4 3) chain B residue 20 type sequence G description binding site for residue ACP B 301 source : AC4 4) chain B residue 21 type sequence G description binding site for residue ACP B 301 source : AC4 5) chain B residue 23 type sequence S description binding site for residue ACP B 301 source : AC4 6) chain B residue 25 type sequence V description binding site for residue ACP B 301 source : AC4 7) chain B residue 38 type sequence A description binding site for residue ACP B 301 source : AC4 8) chain B residue 40 type sequence K description binding site for residue ACP B 301 source : AC4 9) chain B residue 72 type sequence V description binding site for residue ACP B 301 source : AC4 10) chain B residue 92 type sequence M description binding site for residue ACP B 301 source : AC4 11) chain B residue 93 type sequence E description binding site for residue ACP B 301 source : AC4 12) chain B residue 95 type sequence V description binding site for residue ACP B 301 source : AC4 13) chain B residue 99 type sequence T description binding site for residue ACP B 301 source : AC4 14) chain B residue 145 type sequence M description binding site for residue ACP B 301 source : AC4 15) chain B residue 156 type sequence D description binding site for residue MG B 302 source : AC5 16) chain B residue 17 type MOD_RES sequence L description Phosphothreonine; by PknG => ECO:0000269|PubMed:19019160 source Swiss-Prot : SWS_FT_FI2 17) chain B residue 40 type MOD_RES sequence K description Phosphothreonine; by PknG => ECO:0000269|PubMed:19019160 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 93 type MOD_RES sequence E description Phosphothreonine; by PknG => ECO:0000269|PubMed:19019160 source Swiss-Prot : SWS_FT_FI2 19) chain B residue 140 type MOD_RES sequence K description Phosphothreonine; by PknG => ECO:0000269|PubMed:19019160 source Swiss-Prot : SWS_FT_FI2 20) chain B residue 143 type MOD_RES sequence N description Phosphothreonine; by PknB => ECO:0000269|PubMed:15978616 source Swiss-Prot : SWS_FT_FI3 21) chain B residue 156 type MOD_RES sequence D description Phosphothreonine; by PknB => ECO:0000269|PubMed:15978616 source Swiss-Prot : SWS_FT_FI3 22) chain B residue 2 type MOD_RES sequence T description N-acetylthreonine => ECO:0007744|PubMed:21969609 source Swiss-Prot : SWS_FT_FI4 23) chain B residue 169 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000269|PubMed:12548283 source Swiss-Prot : SWS_FT_FI6 24) chain B 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 25) chain B 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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