eF-site ID 3f69-AB PDB Code 3f69 Chain A, B click to enlarge Title Crystal structure of the Mycobacterium tuberculosis PknB mutant kinase domain in complex with KT5720 Classification TRANSFERASE Compound Serine/threonine-protein kinase pknB Source (PKNB_MYCTU) Sequence A:  TPSHLSDRYELGEILGFGGMSEVHLARDLRDHRDVAVKVL RADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAET PAGPLPYIVMEYVDGVTLRDIVHTEGPMTPKRAIEVIADA CQALNFSHQNGIIHRDVKPANILISATNAVKVVDFGIARA ITAQYLSPEQARGDSVDARSDVYSLGCVLYEVLTGEPPFT GDSPVSVAYQHVREDPIPPSARHEGLSADLDAVVLKALAK NPENRYQTAAEMRADLVRVHNGEPPEAPKV B:  TTPSHLSDRYELGEILGFGGMSEVHLARDLRDHRDVAVKV LRADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAE TPAGPLPYIVMEYVDGVTLRDIVHTEGPMTPKRAIEVIAD ACQALNFSHQNGIIHRDVKPANILISATNAVKVVDFGIAR AIADSGNSVXQTIGTAQYLSPEQARGDSVDARSDVYSLGC VLYEVLTGEPPFTGDSPVSVAYQHVREDPIPPSARHEGLS ADLDAVVLKALAKNPENRYQTAAEMRADLVRVHNGEPPEA PKV Description Functional site 1) chain A residue 17 type sequence L description BINDING SITE FOR RESIDUE XDR A 309 source : AC1 2) chain A residue 18 type sequence G description BINDING SITE FOR RESIDUE XDR A 309 source : AC1 3) chain A residue 25 type sequence V description BINDING SITE FOR RESIDUE XDR A 309 source : AC1 4) chain A residue 38 type sequence A description BINDING SITE FOR RESIDUE XDR A 309 source : AC1 5) chain A residue 93 type sequence E description BINDING SITE FOR RESIDUE XDR A 309 source : AC1 6) chain A residue 95 type sequence V description BINDING SITE FOR RESIDUE XDR A 309 source : AC1 7) chain A residue 97 type sequence G description BINDING SITE FOR RESIDUE XDR A 309 source : AC1 8) chain A residue 142 type sequence A description BINDING SITE FOR RESIDUE XDR A 309 source : AC1 9) chain A residue 143 type sequence N description BINDING SITE FOR RESIDUE XDR A 309 source : AC1 10) chain A residue 155 type sequence V description BINDING SITE FOR RESIDUE XDR A 309 source : AC1 11) chain A residue 10 type sequence R description BINDING SITE FOR RESIDUE SO4 A 310 source : AC2 12) chain A residue 32 type sequence R description BINDING SITE FOR RESIDUE SO4 A 310 source : AC2 13) chain A residue 256 type sequence A description BINDING SITE FOR RESIDUE SO4 A 311 source : AC3 14) chain A residue 257 type sequence K description BINDING SITE FOR RESIDUE SO4 A 311 source : AC3 15) chain A residue 258 type sequence N description BINDING SITE FOR RESIDUE SO4 A 311 source : AC3 16) chain A residue 261 type sequence N description BINDING SITE FOR RESIDUE SO4 A 311 source : AC3 17) chain B residue 17 type sequence L description BINDING SITE FOR RESIDUE XDR B 309 source : AC4 18) chain B residue 18 type sequence G description BINDING SITE FOR RESIDUE XDR B 309 source : AC4 19) chain B residue 38 type sequence A description BINDING SITE FOR RESIDUE XDR B 309 source : AC4 20) chain B residue 40 type sequence K description BINDING SITE FOR RESIDUE XDR B 309 source : AC4 21) chain B residue 93 type sequence E description BINDING SITE FOR RESIDUE XDR B 309 source : AC4 22) chain B residue 95 type sequence V description BINDING SITE FOR RESIDUE XDR B 309 source : AC4 23) chain B residue 99 type sequence T description BINDING SITE FOR RESIDUE XDR B 309 source : AC4 24) chain B residue 142 type sequence A description BINDING SITE FOR RESIDUE XDR B 309 source : AC4 25) chain B residue 143 type sequence N description BINDING SITE FOR RESIDUE XDR B 309 source : AC4 26) chain B residue 145 type sequence L description BINDING SITE FOR RESIDUE XDR B 309 source : AC4 27) chain B residue 155 type sequence V description BINDING SITE FOR RESIDUE XDR B 309 source : AC4 28) chain B residue 156 type sequence D description BINDING SITE FOR RESIDUE XDR B 309 source : AC4 29) chain B residue 32 type sequence R description BINDING SITE FOR RESIDUE SO4 B 310 source : AC5 30) chain B residue 256 type sequence A description BINDING SITE FOR RESIDUE SO4 B 311 source : AC6 31) chain B residue 257 type sequence K description BINDING SITE FOR RESIDUE SO4 B 311 source : AC6 32) chain B residue 258 type sequence N description BINDING SITE FOR RESIDUE SO4 B 311 source : AC6 33) chain B residue 261 type sequence N description BINDING SITE FOR RESIDUE SO4 B 311 source : AC6 34) chain B residue 173 type MOD_RES sequence T 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 35) chain B residue 138 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 36) chain A residue 138 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 37) chain B residue 2 type MOD_RES sequence T description N-acetylthreonine => ECO:0007744|PubMed:21969609 source Swiss-Prot : SWS_FT_FI4 38) chain B residue 166 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:15967413 source Swiss-Prot : SWS_FT_FI5 39) chain B residue 169 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000269|PubMed:12548283 source Swiss-Prot : SWS_FT_FI6 40) 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 41) chain A residue 17-40 type prosite sequence LGFGGMSEVHLARDLRDHRDVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGFGGMSEVHlArdlrdhrd..........VAVK source prosite : PS00107 42) chain A residue 134-146 type prosite sequence IIHRDVKPANILI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDVKpaNILI source prosite : PS00108 43) chain A residue 93 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:12551895 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 140 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:12551895 source Swiss-Prot : SWS_FT_FI2 45) chain B residue 17 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:12551895 source Swiss-Prot : SWS_FT_FI2 46) chain B residue 40 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:12551895 source Swiss-Prot : SWS_FT_FI2 47) chain B residue 93 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:12551895 source Swiss-Prot : SWS_FT_FI2 48) chain B residue 140 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:12551895 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 40 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:12551895 source Swiss-Prot : SWS_FT_FI2 50) chain A residue 17 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:12551895 source Swiss-Prot : SWS_FT_FI2 51) chain A residue 143 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 52) chain A residue 156 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 53) chain B residue 143 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 54) chain B residue 156 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3

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