eF-site ID 6i2p-ABCDE PDB Code 6i2p Chain A, B, C, D, E 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 B:  TTPSHLSDRYELGEILGFGGMSEVHLARDLREHRDVAVKV LRADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAE TPAGPLPYIVMEYVDGVTLRDIVHTEGPMTPKRAIEVIAD ACQALNFSHQNGIIHRDVKPANIMISATNAVKVMDFGIAN SVXQXAATAQYLSPEQARGDSVDARSDVYSLGCVLYEVLT GEPPFTGDSPVSVAYQHVREDPIPPSARHEGLSADLDAVV LKALAKNPENRYQTAAEMRADLVRVH C:  XXXXX D:  RADFLSELDSGVEGLPPGSALLVVKRGPNAGSRFLLDQAI TSAGRHPDSDIFLDDVTVSRRHAEFRLENNEFNVVDVGSL NGTYVNREPVDSAVLANGDEVQIGKFRLVFLTGP E:  GVEGLPPGSALLVVKRGPNAGSRFLLDQAITSAGRHPDSD IFLDDVTVSRRHAEFRLENNEFNVVDVGSLNGTYVNREPV DSAVLANGDEVQIGKFRLVFLTGP 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 B residue 18 type sequence G description binding site for residue ACP B 301 source : AC4 21) chain B residue 19 type sequence F description binding site for residue ACP B 301 source : AC4 22) chain B residue 20 type sequence G description binding site for residue ACP B 301 source : AC4 23) chain B residue 21 type sequence G description binding site for residue ACP B 301 source : AC4 24) chain B residue 23 type sequence S description binding site for residue ACP B 301 source : AC4 25) chain B residue 25 type sequence V description binding site for residue ACP B 301 source : AC4 26) chain B residue 38 type sequence A description binding site for residue ACP B 301 source : AC4 27) chain B residue 40 type sequence K description binding site for residue ACP B 301 source : AC4 28) chain B residue 72 type sequence V description binding site for residue ACP B 301 source : AC4 29) chain B residue 92 type sequence M description binding site for residue ACP B 301 source : AC4 30) chain B residue 93 type sequence E description binding site for residue ACP B 301 source : AC4 31) chain B residue 95 type sequence V description binding site for residue ACP B 301 source : AC4 32) chain B residue 99 type sequence T description binding site for residue ACP B 301 source : AC4 33) chain B residue 145 type sequence M description binding site for residue ACP B 301 source : AC4 34) chain B residue 156 type sequence D description binding site for residue MG B 302 source : AC5 35) chain D residue 68 type sequence S description binding site for residue SO4 D 201 source : AC6 36) chain D residue 69 type sequence R description binding site for residue SO4 D 201 source : AC6 37) chain A residue 137 type sequence R description binding site for residue SO4 D 202 source : AC7 38) chain D residue 91 type sequence D description binding site for residue SO4 D 202 source : AC7 39) chain D residue 92 type sequence V description binding site for residue SO4 D 202 source : AC7 40) chain D residue 141 type sequence K description binding site for residue SO4 D 202 source : AC7 41) chain A residue 93 type MOD_RES sequence E description Phosphothreonine; by PknG => ECO:0000269|PubMed:19019160 source Swiss-Prot : SWS_FT_FI2 42) chain A residue 140 type MOD_RES sequence K description Phosphothreonine; by PknG => ECO:0000269|PubMed:19019160 source Swiss-Prot : SWS_FT_FI2 43) chain B residue 17 type MOD_RES sequence L description Phosphothreonine; by PknG => ECO:0000269|PubMed:19019160 source Swiss-Prot : SWS_FT_FI2 44) chain B residue 40 type MOD_RES sequence K description Phosphothreonine; by PknG => ECO:0000269|PubMed:19019160 source Swiss-Prot : SWS_FT_FI2 45) chain B residue 93 type MOD_RES sequence E description Phosphothreonine; by PknG => ECO:0000269|PubMed:19019160 source Swiss-Prot : SWS_FT_FI2 46) chain B residue 140 type MOD_RES sequence K description Phosphothreonine; by PknG => ECO:0000269|PubMed:19019160 source Swiss-Prot : SWS_FT_FI2 47) chain B residue 143 type MOD_RES sequence N description Phosphothreonine; by PknB => ECO:0000269|PubMed:15978616 source Swiss-Prot : SWS_FT_FI3 48) chain B residue 156 type MOD_RES sequence D description Phosphothreonine; by PknB => ECO:0000269|PubMed:15978616 source Swiss-Prot : SWS_FT_FI3 49) chain A residue 17-40 type prosite sequence LGFGGMSEVHLARDLREHRDVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGFGGMSEVHlArdlrehrd..........VAVK source prosite : PS00107 50) chain A residue 134-146 type prosite sequence IIHRDVKPANIMI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDVKpaNIMI source prosite : PS00108 51) chain A residue 2 type MOD_RES sequence T description N-acetylthreonine => ECO:0007744|PubMed:21969609 source Swiss-Prot : SWS_FT_FI4 52) chain B residue 2 type MOD_RES sequence T description N-acetylthreonine => ECO:0007744|PubMed:21969609 source Swiss-Prot : SWS_FT_FI4 53) chain A residue 169 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000269|PubMed:12548283 source Swiss-Prot : SWS_FT_FI6 54) chain B residue 169 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000269|PubMed:12548283 source Swiss-Prot : SWS_FT_FI6 55) 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 56) 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 57) 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 58) 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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