eF-site ID 2xkp-ABCDEF PDB Code 2xkp Chain A, B, C, D, E, F click to enlarge Title NtcA from Synechococcus elongatus: active and inactive Classification TRANSCRIPTION Compound GLOBAL NITROGEN REGULATOR Source Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2) (NTCA_SYNE7) Sequence A:  ENSLLTMFREIEQFERGKTIFFPGDPAERVYLLVKGAVKL SRVYESGEEITVALLRENSVFGVLSLLTRSDRFYHAVAFT PVQLFSVPIEFMQKALIERPELANVMLQGLSSRILQTEMM IETLAHRDMGSRLVSFLLILCRDFGIPSPDGITIDLKLSH QAIAEAIGSTRVTVTRLLGDLRESKLIAIHKKRITVFNPV ALSQQFS B:  NSLLTMFRELKLPLQIEQFERGKTIFFPGDPAERVYLLVK GAVKLSRVYESGEEITVALLRENSVFGVLSLLTGRSDRFY HAVAFTPVQLFSVPIEFMQKALIERPELANVMLQGLSSRI LQTEMMIETLAHRDMGSRLVSFLLILCRDFGIPSPDGITI DLKLSHQAIAEAIGSTRVTVTRLLGDLRESKLIAIHKKRI TVFNPVALSQQ C:  PLQIEQFERGKTIFFPGDPAERVYLLVKGAVKLSRVYESG EEITVALLRENSVFGVLSLLRSDRFYHAVAFTPVQLFSVP IEFMQKALIERPELANVMLQGLSSRILQTEMMIETLAHRD MGSRLVSFLLILCRDFGIPSPDGITIDLKLSHQAIAEAIG STRVTVTRLLGDLRESKLIAIHKKRITVFNPVALSQ D:  ENSLLTMFREIEQFERGKTIFFPGDPAERVYLLVKGAVKL SRVYESGEEITVALLRENSVFGVLSLLTRSDRFYHAVAFT PVQLFSVPIEFMQKALIERPELANVMLQGLSSRILQTEMM IETLAHRDMGSRLVSFLLILCRDFGIPSPDGITIDLKLSH QAIAEAIGSTRVTVTRLLGDLRESKLIAIHKKRITVFNPV ALSQQFS E:  NSLLTMFRELKLPLQIEQFERGKTIFFPGDPAERVYLLVK GAVKLSRVYESGEEITVALLRENSVFGVLSLLTGRSDRFY HAVAFTPVQLFSVPIEFMQKALIERPELANVMLQGLSSRI LQTEMMIETLAHRDMGSRLVSFLLILCRDFGIPSPDGITI DLKLSHQAIAEAIGSTRVTVTRLLGDLRESKLIAIHKKRI TVFNPVALSQQ F:  PLQIEQFERGKTIFFPGDPAERVYLLVKGAVKLSRVYESG EEITVALLRENSVFGVLSLLRSDRFYHAVAFTPVQLFSVP IEFMQKALIERPELANVMLQGLSSRILQTEMMIETLAHRD MGSRLVSFLLILCRDFGIPSPDGITIDLKLSHQAIAEAIG STRVTVTRLLGDLRESKLIAIHKKRITVFNPVALSQ Description Functional site 1) chain A residue 53 type sequence L description BINDING SITE FOR RESIDUE AKG A 1223 source : AC1 2) chain A residue 74 type sequence F description BINDING SITE FOR RESIDUE AKG A 1223 source : AC1 3) chain A residue 75 type sequence G description BINDING SITE FOR RESIDUE AKG A 1223 source : AC1 4) chain A residue 76 type sequence V description BINDING SITE FOR RESIDUE AKG A 1223 source : AC1 5) chain A residue 77 type sequence L description BINDING SITE FOR RESIDUE AKG A 1223 source : AC1 6) chain A residue 87 type sequence R description BINDING SITE FOR RESIDUE AKG A 1223 source : AC1 7) chain A residue 88 type sequence F description BINDING SITE FOR RESIDUE AKG A 1223 source : AC1 8) chain A residue 89 type sequence Y description BINDING SITE FOR RESIDUE AKG A 1223 source : AC1 9) chain A residue 128 type sequence R description BINDING SITE FOR RESIDUE AKG A 1223 source : AC1 10) chain B residue 133 type sequence E description BINDING SITE FOR RESIDUE AKG A 1223 source : AC1 11) chain A residue 130 type sequence L description BINDING SITE FOR RESIDUE AKG B 1221 source : AC2 12) chain A residue 133 type sequence E description BINDING SITE FOR RESIDUE AKG B 1221 source : AC2 13) chain B residue 53 type sequence L description BINDING SITE FOR RESIDUE AKG B 1221 source : AC2 14) chain B residue 74 type sequence F description BINDING SITE FOR RESIDUE AKG B 1221 source : AC2 15) chain B residue 75 type sequence G description BINDING SITE FOR RESIDUE AKG B 1221 source : AC2 16) chain B residue 76 type sequence V description BINDING SITE FOR RESIDUE AKG B 1221 source : AC2 17) chain B residue 77 type sequence L description BINDING SITE FOR RESIDUE AKG B 1221 source : AC2 18) chain B residue 87 type sequence R description BINDING SITE FOR RESIDUE AKG B 1221 source : AC2 19) chain B residue 88 type sequence F description BINDING SITE FOR RESIDUE AKG B 1221 source : AC2 20) chain B residue 89 type sequence Y description BINDING SITE FOR RESIDUE AKG B 1221 source : AC2 21) chain B residue 128 type sequence R description BINDING SITE FOR RESIDUE AKG B 1221 source : AC2 22) chain C residue 74 type sequence F description BINDING SITE FOR RESIDUE AKG C 1220 source : AC3 23) chain C residue 75 type sequence G description BINDING SITE FOR RESIDUE AKG C 1220 source : AC3 24) chain C residue 76 type sequence V description BINDING SITE FOR RESIDUE AKG C 1220 source : AC3 25) chain C residue 77 type sequence L description BINDING SITE FOR RESIDUE AKG C 1220 source : AC3 26) chain C residue 87 type sequence R description BINDING SITE FOR RESIDUE AKG C 1220 source : AC3 27) chain C residue 88 type sequence F description BINDING SITE FOR RESIDUE AKG C 1220 source : AC3 28) chain C residue 89 type sequence Y description BINDING SITE FOR RESIDUE AKG C 1220 source : AC3 29) chain C residue 128 type sequence R description BINDING SITE FOR RESIDUE AKG C 1220 source : AC3 30) chain D residue 53 type sequence L description BINDING SITE FOR RESIDUE AKG D 1223 source : AC4 31) chain D residue 74 type sequence F description BINDING SITE FOR RESIDUE AKG D 1223 source : AC4 32) chain D residue 75 type sequence G description BINDING SITE FOR RESIDUE AKG D 1223 source : AC4 33) chain D residue 76 type sequence V description BINDING SITE FOR RESIDUE AKG D 1223 source : AC4 34) chain D residue 77 type sequence L description BINDING SITE FOR RESIDUE AKG D 1223 source : AC4 35) chain D residue 87 type sequence R description BINDING SITE FOR RESIDUE AKG D 1223 source : AC4 36) chain D residue 88 type sequence F description BINDING SITE FOR RESIDUE AKG D 1223 source : AC4 37) chain D residue 89 type sequence Y description BINDING SITE FOR RESIDUE AKG D 1223 source : AC4 38) chain D residue 128 type sequence R description BINDING SITE FOR RESIDUE AKG D 1223 source : AC4 39) chain E residue 133 type sequence E description BINDING SITE FOR RESIDUE AKG D 1223 source : AC4 40) chain D residue 130 type sequence L description BINDING SITE FOR RESIDUE AKG E 1221 source : AC5 41) chain D residue 133 type sequence E description BINDING SITE FOR RESIDUE AKG E 1221 source : AC5 42) chain E residue 53 type sequence L description BINDING SITE FOR RESIDUE AKG E 1221 source : AC5 43) chain E residue 74 type sequence F description BINDING SITE FOR RESIDUE AKG E 1221 source : AC5 44) chain E residue 75 type sequence G description BINDING SITE FOR RESIDUE AKG E 1221 source : AC5 45) chain E residue 76 type sequence V description BINDING SITE FOR RESIDUE AKG E 1221 source : AC5 46) chain E residue 77 type sequence L description BINDING SITE FOR RESIDUE AKG E 1221 source : AC5 47) chain E residue 87 type sequence R description BINDING SITE FOR RESIDUE AKG E 1221 source : AC5 48) chain E residue 88 type sequence F description BINDING SITE FOR RESIDUE AKG E 1221 source : AC5 49) chain E residue 89 type sequence Y description BINDING SITE FOR RESIDUE AKG E 1221 source : AC5 50) chain E residue 128 type sequence R description BINDING SITE FOR RESIDUE AKG E 1221 source : AC5 51) chain F residue 74 type sequence F description BINDING SITE FOR RESIDUE AKG F 1220 source : AC6 52) chain F residue 75 type sequence G description BINDING SITE FOR RESIDUE AKG F 1220 source : AC6 53) chain F residue 76 type sequence V description BINDING SITE FOR RESIDUE AKG F 1220 source : AC6 54) chain F residue 77 type sequence L description BINDING SITE FOR RESIDUE AKG F 1220 source : AC6 55) chain F residue 78 type sequence S description BINDING SITE FOR RESIDUE AKG F 1220 source : AC6 56) chain F residue 87 type sequence R description BINDING SITE FOR RESIDUE AKG F 1220 source : AC6 57) chain F residue 88 type sequence F description BINDING SITE FOR RESIDUE AKG F 1220 source : AC6 58) chain F residue 89 type sequence Y description BINDING SITE FOR RESIDUE AKG F 1220 source : AC6 59) chain F residue 128 type sequence R description BINDING SITE FOR RESIDUE AKG F 1220 source : AC6 60) chain A residue 173-196 type prosite sequence LSHQAIAEAIGSTRVTVTRLLGDL description HTH_CRP_1 Crp-type HTH domain signature. LSHqaIAeAIGsTrvTv.TRlLgdL source prosite : PS00042 61) chain A residue 175-194 type DNA_BIND sequence HQAIAEAIGSTRVTVTRLLG description H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00387 source Swiss-Prot : SWS_FT_FI1 62) chain B residue 175-194 type DNA_BIND sequence HQAIAEAIGSTRVTVTRLLG description H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00387 source Swiss-Prot : SWS_FT_FI1 63) chain C residue 175-194 type DNA_BIND sequence HQAIAEAIGSTRVTVTRLLG description H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00387 source Swiss-Prot : SWS_FT_FI1 64) chain D residue 175-194 type DNA_BIND sequence HQAIAEAIGSTRVTVTRLLG description H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00387 source Swiss-Prot : SWS_FT_FI1 65) chain E residue 175-194 type DNA_BIND sequence HQAIAEAIGSTRVTVTRLLG description H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00387 source Swiss-Prot : SWS_FT_FI1 66) chain F residue 175-194 type DNA_BIND sequence HQAIAEAIGSTRVTVTRLLG description H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00387 source Swiss-Prot : SWS_FT_FI1 67) chain A residue 6 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 68) chain B residue 6 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 69) chain D residue 6 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 70) chain E residue 6 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2

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