eF-site ID 1ojl-ABCDEF PDB Code 1ojl Chain A, B, C, D, E, F click to enlarge Title Crystal structure of a sigma54-activator suggests the mechanism for the conformational switch necessary for sigma54 binding Classification RESPONSE REGULATOR Compound TRANSCRIPTIONAL REGULATORY PROTEIN ZRAR Source (ZRAR_SALTY) Sequence A:  HMIGSSPAMQHLLNEIAMVAPSDATVLIHGDSGTGKELVA RALHACSARSDRPLVTLNCAALNESLLESELFGHEKGAFT KRREGRFVEADGGTLFLDEIGDISPLMQVRLLRAIQEREV QRVGSNQTISVDVRLIAATHRDLAEEVSAGRFRQDLYYRL NVVAIEMPSLRQRREDIPLLADHFLRRFAERNRKVVKGFT PQAMDLLIHYDWPGNIRELENAIERAVVLLTGEYISEREL PLAIAYSGEIQPLVDVEKEVILAALEKTGGNKTEAARQLG ITRKTLLAKLSR B:  SHMIGSSPAMQHLLNEIAMVAPSDATVLIHGDSGTGKELV ARALHACSARSDRPLVTLNCAALNESLLESELFGHEKGAF TGADKRREGRFVEADGGTLFLDEIGDISPLMQVRLLRAIQ EREVQRVGSNQTISVDVRLIAATHRDLAEEVSAGRFRQDL YYRLNVVAIEMPSLRQRREDIPLLADHFLRRFAERNRKVV KGFTPQAMDLLIHYDWPGNIRELENAIERAVVLLTGEYIS ERELPLAIAAT C:  SHMIGSSPAMQHLLNEIAMVAPSDATVLIHGDSGTGKELV ARALHACSARSDRPLVTLNCAALNESLLESELFGHEKGAF TGADKRREGRFVEADGGTLFLDEIGDISPLMQVRLLRAIQ EREVQRVGSNQTISVDVRLIAATHRDLAEEVSAGRFRQDL YYRLNVVAIEMPSLRQRREDIPLLADHFLRRFAERNRKVV KGFTPQAMDLLIHYDWPGNIRELENAIERAVVLLTGEYIS ERELPLAIAATP D:  HMIGSSPAMQHLLNEIAMVAPSDATVLIHGDSGTGKELVA RALHACSARSDRPLVTLNCAALNESLLESELFGHEKGAFT GADKRREGRFVEADGGTLFLDEIGDISPLMQVRLLRAIQE REVQRVGSNQTISVDVRLIAATHRDLAEEVSAGRFRQDLY YRLNVVAIEMPSLRQRREDIPLLADHFLRRFAERNRKVVK GFTPQAMDLLIHYDWPGNIRELENAIERAVVLLTGEYISE RELPLAIAATPIKEIQPLVDVEKEVILAALEKTGGNKTEA ARQLGITRKTLLAKLSR E:  HMIGSSPAMQHLLNEIAMVAPSDATVLIHGDSGTGKELVA RALHACSARSDRPLVTLNCAALNESLLESELFGHEKGAFT KRREGRFVEADGGTLFLDEIGDISPLMQVRLLRAIQEREV QRVGSNQTISVDVRLIAATHRDLAEEVSAGRFRQDLYYRL NVVAIEMPSLRQRREDIPLLADHFLRRFAERNRKVVKGFT PQAMDLLIHYDWPGNIRELENAIERAVVLLTGEYISEREL PLAIPLVDVEKEVILAALEKTGGNKTEAARQLGITRKTLL AKLSR F:  HMIGSSPAMQHLLNEIAMVAPSDATVLIHGDSGTGKELVA RALHACSARSDRPLVTLNCAALNESLLESELFGHEKGAFT KRREGRFVEADGGTLFLDEIGDISPLMQVRLLRAIQEREV QRVGSNQTISVDVRLIAATHRDLAEEVSAGRFRQDLYYRL NVVAIEMPSLRQRREDIPLLADHFLRRFAERNRKVVKGFT PQAMDLLIHYDWPGNIRELENAIERAVVLLTGEYISEREL PLAIAAT Description (1)  TRANSCRIPTIONAL REGULATORY PROTEIN ZRAR Functional site 1) chain A residue 171 type sequence S description BINDING SITE FOR RESIDUE PO4 A1442 source : AC1 2) chain A residue 172 type sequence G description BINDING SITE FOR RESIDUE PO4 A1442 source : AC1 3) chain A residue 173 type sequence T description BINDING SITE FOR RESIDUE PO4 A1442 source : AC1 4) chain A residue 175 type sequence K description BINDING SITE FOR RESIDUE PO4 A1442 source : AC1 5) chain A residue 359 type sequence R description BINDING SITE FOR RESIDUE PO4 A1442 source : AC1 6) chain B residue 171 type sequence S description BINDING SITE FOR RESIDUE PO4 B1390 source : AC2 7) chain B residue 172 type sequence G description BINDING SITE FOR RESIDUE PO4 B1390 source : AC2 8) chain B residue 173 type sequence T description BINDING SITE FOR RESIDUE PO4 B1390 source : AC2 9) chain B residue 175 type sequence K description BINDING SITE FOR RESIDUE PO4 B1390 source : AC2 10) chain B residue 359 type sequence R description BINDING SITE FOR RESIDUE PO4 B1390 source : AC2 11) chain C residue 170 type sequence D description BINDING SITE FOR RESIDUE PO4 C1391 source : AC3 12) chain C residue 171 type sequence S description BINDING SITE FOR RESIDUE PO4 C1391 source : AC3 13) chain C residue 172 type sequence G description BINDING SITE FOR RESIDUE PO4 C1391 source : AC3 14) chain C residue 173 type sequence T description BINDING SITE FOR RESIDUE PO4 C1391 source : AC3 15) chain C residue 175 type sequence K description BINDING SITE FOR RESIDUE PO4 C1391 source : AC3 16) chain C residue 359 type sequence R description BINDING SITE FOR RESIDUE PO4 C1391 source : AC3 17) chain D residue 171 type sequence S description BINDING SITE FOR RESIDUE PO4 D1442 source : AC4 18) chain D residue 172 type sequence G description BINDING SITE FOR RESIDUE PO4 D1442 source : AC4 19) chain D residue 173 type sequence T description BINDING SITE FOR RESIDUE PO4 D1442 source : AC4 20) chain D residue 175 type sequence K description BINDING SITE FOR RESIDUE PO4 D1442 source : AC4 21) chain D residue 359 type sequence R description BINDING SITE FOR RESIDUE PO4 D1442 source : AC4 22) chain F residue 171 type sequence S description BINDING SITE FOR RESIDUE PO4 F1390 source : AC5 23) chain F residue 172 type sequence G description BINDING SITE FOR RESIDUE PO4 F1390 source : AC5 24) chain F residue 173 type sequence T description BINDING SITE FOR RESIDUE PO4 F1390 source : AC5 25) chain F residue 175 type sequence K description BINDING SITE FOR RESIDUE PO4 F1390 source : AC5 26) chain F residue 176 type sequence E description BINDING SITE FOR RESIDUE PO4 F1390 source : AC5 27) chain F residue 240 type sequence D description BINDING SITE FOR RESIDUE PO4 F1390 source : AC5 28) chain F residue 359 type sequence R description BINDING SITE FOR RESIDUE PO4 F1390 source : AC5 29) chain E residue 142 type sequence I description BINDING SITE FOR RESIDUE ATP E1442 source : AC6 30) chain E residue 171 type sequence S description BINDING SITE FOR RESIDUE ATP E1442 source : AC6 31) chain E residue 172 type sequence G description BINDING SITE FOR RESIDUE ATP E1442 source : AC6 32) chain E residue 173 type sequence T description BINDING SITE FOR RESIDUE ATP E1442 source : AC6 33) chain E residue 174 type sequence G description BINDING SITE FOR RESIDUE ATP E1442 source : AC6 34) chain E residue 175 type sequence K description BINDING SITE FOR RESIDUE ATP E1442 source : AC6 35) chain E residue 176 type sequence E description BINDING SITE FOR RESIDUE ATP E1442 source : AC6 36) chain E residue 240 type sequence D description BINDING SITE FOR RESIDUE ATP E1442 source : AC6 37) chain E residue 315 type sequence R description BINDING SITE FOR RESIDUE ATP E1442 source : AC6 38) chain E residue 322 type sequence L description BINDING SITE FOR RESIDUE ATP E1442 source : AC6 39) chain E residue 326 type sequence F description BINDING SITE FOR RESIDUE ATP E1442 source : AC6 40) chain E residue 329 type sequence R description BINDING SITE FOR RESIDUE ATP E1442 source : AC6 41) chain E residue 358 type sequence I description BINDING SITE FOR RESIDUE ATP E1442 source : AC6 42) chain E residue 359 type sequence R description BINDING SITE FOR RESIDUE ATP E1442 source : AC6 43) chain E residue 362 type sequence E description BINDING SITE FOR RESIDUE ATP E1442 source : AC6 44) chain A residue 421-440 type DNA_BIND sequence KTEAARQLGITRKTLLAKLS description H-T-H motif => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 45) chain D residue 421-440 type DNA_BIND sequence KTEAARQLGITRKTLLAKLS description H-T-H motif => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 46) chain E residue 421-440 type DNA_BIND sequence KTEAARQLGITRKTLLAKLS description H-T-H motif => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 47) chain A residue 169 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00193 source Swiss-Prot : SWS_FT_FI2 48) chain A residue 232 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00193 source Swiss-Prot : SWS_FT_FI2 49) chain C residue 169 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00193 source Swiss-Prot : SWS_FT_FI2 50) chain E residue 232 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00193 source Swiss-Prot : SWS_FT_FI2 51) chain F residue 169 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00193 source Swiss-Prot : SWS_FT_FI2 52) chain F residue 232 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00193 source Swiss-Prot : SWS_FT_FI2 53) chain D residue 169 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00193 source Swiss-Prot : SWS_FT_FI2 54) chain D residue 232 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00193 source Swiss-Prot : SWS_FT_FI2 55) chain E residue 169 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00193 source Swiss-Prot : SWS_FT_FI2 56) chain B residue 169 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00193 source Swiss-Prot : SWS_FT_FI2 57) chain B residue 232 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00193 source Swiss-Prot : SWS_FT_FI2 58) chain C residue 232 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00193 source Swiss-Prot : SWS_FT_FI2 59) chain A residue 165-178 type prosite sequence VLIHGDSGTGKELV description SIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. VLIhGDSGTGKelV source prosite : PS00675 60) chain A residue 227-242 type prosite sequence GRFVEADGGTLFLDEI description SIGMA54_INTERACT_2 Sigma-54 interaction domain ATP-binding region B signature. GrFveADGGTLFLDEI source prosite : PS00676 61) chain A residue 354-363 type prosite sequence WPGNIRELEN description SIGMA54_INTERACT_3 Sigma-54 interaction domain C-terminal part signature. WPGNIRELeN source prosite : PS00688

Display surface Download Links