eF-site ID 2xr8-ABCDEFGHIJKLMNOPQRSTUVWX PDB Code 2xr8 Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X Title Crystal structure of biphenyl dioxygenase from Burkholderia xenovorans LB400 Classification OXIDOREDUCTASE Compound BIPHENYL DIOXYGENASE SUBUNIT ALPHA Source Burkholderia xenovorans (strain LB400) (BPHE_BURXL) Sequence A:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPTFNNIRIWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP B:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF C:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPTFNNIRIWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP D:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF E:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPTFNNIRIWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP F:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF G:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPTFNNIRIWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP H:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF I:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPTFNNIRIWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP J:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF K:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPTFNNIRIWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP L:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF M:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPTFNNIRIWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP N:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF O:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPTFNNIRIWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP P:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF Q:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPTFNNIRIWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP R:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF S:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPTFNNIRIWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP T:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF U:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPTFNNIRIWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP V:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF W:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPTFNNIRIWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP X:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF Description Functional site 1) chain A residue 100 type sequence C description BINDING SITE FOR RESIDUE FES A 900 source : AC1 2) chain A residue 102 type sequence H description BINDING SITE FOR RESIDUE FES A 900 source : AC1 3) chain A residue 103 type sequence R description BINDING SITE FOR RESIDUE FES A 900 source : AC1 4) chain A residue 120 type sequence C description BINDING SITE FOR RESIDUE FES A 900 source : AC1 5) chain A residue 123 type sequence H description BINDING SITE FOR RESIDUE FES A 900 source : AC1 6) chain A residue 125 type sequence W description BINDING SITE FOR RESIDUE FES A 900 source : AC1 7) chain A residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 A 901 source : AC2 8) chain A residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 A 901 source : AC2 9) chain A residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 A 901 source : AC2 10) chain A residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 A 901 source : AC2 11) chain C residue 100 type sequence C description BINDING SITE FOR RESIDUE FES C 900 source : AC3 12) chain C residue 102 type sequence H description BINDING SITE FOR RESIDUE FES C 900 source : AC3 13) chain C residue 103 type sequence R description BINDING SITE FOR RESIDUE FES C 900 source : AC3 14) chain C residue 120 type sequence C description BINDING SITE FOR RESIDUE FES C 900 source : AC3 15) chain C residue 123 type sequence H description BINDING SITE FOR RESIDUE FES C 900 source : AC3 16) chain C residue 125 type sequence W description BINDING SITE FOR RESIDUE FES C 900 source : AC3 17) chain C residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 C 901 source : AC4 18) chain C residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 C 901 source : AC4 19) chain C residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 C 901 source : AC4 20) chain C residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 C 901 source : AC4 21) chain E residue 100 type sequence C description BINDING SITE FOR RESIDUE FES E 900 source : AC5 22) chain E residue 102 type sequence H description BINDING SITE FOR RESIDUE FES E 900 source : AC5 23) chain E residue 103 type sequence R description BINDING SITE FOR RESIDUE FES E 900 source : AC5 24) chain E residue 120 type sequence C description BINDING SITE FOR RESIDUE FES E 900 source : AC5 25) chain E residue 123 type sequence H description BINDING SITE FOR RESIDUE FES E 900 source : AC5 26) chain E residue 125 type sequence W description BINDING SITE FOR RESIDUE FES E 900 source : AC5 27) chain E residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 E 901 source : AC6 28) chain E residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 E 901 source : AC6 29) chain E residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 E 901 source : AC6 30) chain E residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 E 901 source : AC6 31) chain G residue 100 type sequence C description BINDING SITE FOR RESIDUE FES G 900 source : AC7 32) chain G residue 102 type sequence H description BINDING SITE FOR RESIDUE FES G 900 source : AC7 33) chain G residue 103 type sequence R description BINDING SITE FOR RESIDUE FES G 900 source : AC7 34) chain G residue 120 type sequence C description BINDING SITE FOR RESIDUE FES G 900 source : AC7 35) chain G residue 123 type sequence H description BINDING SITE FOR RESIDUE FES G 900 source : AC7 36) chain G residue 125 type sequence W description BINDING SITE FOR RESIDUE FES G 900 source : AC7 37) chain G residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 G 901 source : AC8 38) chain G residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 G 901 source : AC8 39) chain G residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 G 901 source : AC8 40) chain G residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 G 901 source : AC8 41) chain I residue 100 type sequence C description BINDING SITE FOR RESIDUE FES I 900 source : AC9 42) chain I residue 102 type sequence H description BINDING SITE FOR RESIDUE FES I 900 source : AC9 43) chain I residue 103 type sequence R description BINDING SITE FOR RESIDUE FES I 900 source : AC9 44) chain I residue 105 type sequence M description BINDING SITE FOR RESIDUE FES I 900 source : AC9 45) chain I residue 120 type sequence C description BINDING SITE FOR RESIDUE FES I 900 source : AC9 46) chain I residue 123 type sequence H description BINDING SITE FOR RESIDUE FES I 900 source : AC9 47) chain I residue 125 type sequence W description BINDING SITE FOR RESIDUE FES I 900 source : AC9 48) chain I residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 I 901 source : BC1 49) chain I residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 I 901 source : BC1 50) chain I residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 I 901 source : BC1 51) chain I residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 I 901 source : BC1 52) chain K residue 100 type sequence C description BINDING SITE FOR RESIDUE FES K 900 source : BC2 53) chain K residue 102 type sequence H description BINDING SITE FOR RESIDUE FES K 900 source : BC2 54) chain K residue 103 type sequence R description BINDING SITE FOR RESIDUE FES K 900 source : BC2 55) chain K residue 105 type sequence M description BINDING SITE FOR RESIDUE FES K 900 source : BC2 56) chain K residue 120 type sequence C description BINDING SITE FOR RESIDUE FES K 900 source : BC2 57) chain K residue 123 type sequence H description BINDING SITE FOR RESIDUE FES K 900 source : BC2 58) chain K residue 125 type sequence W description BINDING SITE FOR RESIDUE FES K 900 source : BC2 59) chain K residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 K 901 source : BC3 60) chain K residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 K 901 source : BC3 61) chain K residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 K 901 source : BC3 62) chain M residue 100 type sequence C description BINDING SITE FOR RESIDUE FES M 900 source : BC4 63) chain M residue 102 type sequence H description BINDING SITE FOR RESIDUE FES M 900 source : BC4 64) chain M residue 103 type sequence R description BINDING SITE FOR RESIDUE FES M 900 source : BC4 65) chain M residue 120 type sequence C description BINDING SITE FOR RESIDUE FES M 900 source : BC4 66) chain M residue 123 type sequence H description BINDING SITE FOR RESIDUE FES M 900 source : BC4 67) chain M residue 125 type sequence W description BINDING SITE FOR RESIDUE FES M 900 source : BC4 68) chain M residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 M 901 source : BC5 69) chain M residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 M 901 source : BC5 70) chain M residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 M 901 source : BC5 71) chain O residue 100 type sequence C description BINDING SITE FOR RESIDUE FES O 900 source : BC6 72) chain O residue 102 type sequence H description BINDING SITE FOR RESIDUE FES O 900 source : BC6 73) chain O residue 103 type sequence R description BINDING SITE FOR RESIDUE FES O 900 source : BC6 74) chain O residue 120 type sequence C description BINDING SITE FOR RESIDUE FES O 900 source : BC6 75) chain O residue 123 type sequence H description BINDING SITE FOR RESIDUE FES O 900 source : BC6 76) chain O residue 125 type sequence W description BINDING SITE FOR RESIDUE FES O 900 source : BC6 77) chain O residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 O 901 source : BC7 78) chain O residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 O 901 source : BC7 79) chain O residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 O 901 source : BC7 80) chain O residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 O 901 source : BC7 81) chain Q residue 100 type sequence C description BINDING SITE FOR RESIDUE FES Q 900 source : BC8 82) chain Q residue 102 type sequence H description BINDING SITE FOR RESIDUE FES Q 900 source : BC8 83) chain Q residue 103 type sequence R description BINDING SITE FOR RESIDUE FES Q 900 source : BC8 84) chain Q residue 120 type sequence C description BINDING SITE FOR RESIDUE FES Q 900 source : BC8 85) chain Q residue 123 type sequence H description BINDING SITE FOR RESIDUE FES Q 900 source : BC8 86) chain Q residue 125 type sequence W description BINDING SITE FOR RESIDUE FES Q 900 source : BC8 87) chain Q residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 Q 901 source : BC9 88) chain Q residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 Q 901 source : BC9 89) chain Q residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 Q 901 source : BC9 90) chain Q residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 Q 901 source : BC9 91) chain S residue 100 type sequence C description BINDING SITE FOR RESIDUE FES S 900 source : CC1 92) chain S residue 102 type sequence H description BINDING SITE FOR RESIDUE FES S 900 source : CC1 93) chain S residue 103 type sequence R description BINDING SITE FOR RESIDUE FES S 900 source : CC1 94) chain S residue 120 type sequence C description BINDING SITE FOR RESIDUE FES S 900 source : CC1 95) chain S residue 123 type sequence H description BINDING SITE FOR RESIDUE FES S 900 source : CC1 96) chain S residue 125 type sequence W description BINDING SITE FOR RESIDUE FES S 900 source : CC1 97) chain S residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 S 901 source : CC2 98) chain S residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 S 901 source : CC2 99) chain S residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 S 901 source : CC2 100) chain S residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 S 901 source : CC2 101) chain U residue 100 type sequence C description BINDING SITE FOR RESIDUE FES U 900 source : CC3 102) chain U residue 102 type sequence H description BINDING SITE FOR RESIDUE FES U 900 source : CC3 103) chain U residue 103 type sequence R description BINDING SITE FOR RESIDUE FES U 900 source : CC3 104) chain U residue 120 type sequence C description BINDING SITE FOR RESIDUE FES U 900 source : CC3 105) chain U residue 122 type sequence Y description BINDING SITE FOR RESIDUE FES U 900 source : CC3 106) chain U residue 123 type sequence H description BINDING SITE FOR RESIDUE FES U 900 source : CC3 107) chain U residue 125 type sequence W description BINDING SITE FOR RESIDUE FES U 900 source : CC3 108) chain U residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 U 901 source : CC4 109) chain U residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 U 901 source : CC4 110) chain U residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 U 901 source : CC4 111) chain U residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 U 901 source : CC4 112) chain W residue 100 type sequence C description BINDING SITE FOR RESIDUE FES W 900 source : CC5 113) chain W residue 102 type sequence H description BINDING SITE FOR RESIDUE FES W 900 source : CC5 114) chain W residue 103 type sequence R description BINDING SITE FOR RESIDUE FES W 900 source : CC5 115) chain W residue 120 type sequence C description BINDING SITE FOR RESIDUE FES W 900 source : CC5 116) chain W residue 123 type sequence H description BINDING SITE FOR RESIDUE FES W 900 source : CC5 117) chain W residue 125 type sequence W description BINDING SITE FOR RESIDUE FES W 900 source : CC5 118) chain W residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 W 901 source : CC6 119) chain W residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 W 901 source : CC6 120) chain W residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 W 901 source : CC6 121) chain W residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 W 901 source : CC6 122) chain A residue 100-123 type prosite sequence CRHRGMRICRSDAGNAKAFTCSYH description RING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CrHRGmricrsdaGNakaftCsYH source prosite : PS00570 123) chain A residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 124) chain E residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 125) chain E residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 126) chain E residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 127) chain G residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 128) chain G residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 129) chain G residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 130) chain G residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 131) chain I residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 132) chain I residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 133) chain I residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 134) chain A residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 135) chain I residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 136) chain K residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 137) chain K residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 138) chain K residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 139) chain K residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 140) chain M residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 141) chain M residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 142) chain M residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 143) chain M residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 144) chain O residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 145) chain A residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 146) chain O residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 147) chain O residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 148) chain O residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 149) chain Q residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 150) chain Q residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 151) chain Q residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 152) chain Q residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 153) chain S residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 154) chain S residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 155) chain S residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 156) chain A residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 157) chain S residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 158) chain U residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 159) chain U residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 160) chain U residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 161) chain U residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 162) chain W residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 163) chain W residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 164) chain W residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 165) chain W residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 166) chain C residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 167) chain C residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 168) chain C residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 169) chain C residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 170) chain E residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 171) chain A residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 172) chain I residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 173) chain K residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 174) chain K residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 175) chain M residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 176) chain M residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 177) chain O residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 178) chain O residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 179) chain Q residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 180) chain Q residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 181) chain S residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 182) chain A residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 183) chain S residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 184) chain U residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 185) chain U residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 186) chain W residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 187) chain W residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 188) chain C residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 189) chain C residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 190) chain E residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 191) chain E residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 192) chain G residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 193) chain G residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 194) chain I residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2

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