eF-site ID 5aew-ABCDEFGHIJKLMNOPQRSTUVWX PDB Code 5aew 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 II9 variant of Biphenyl dioxygenase from Burkholderia xenovorans LB400 in complex with biphenyl Classification OXIDOREDUCTASE Compound BIPHENYL DIOXYGENASE SUBUNIT ALPHA Source (BPHE_BURXL) Sequence A:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPGINTIRTWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP B:  PHFFKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEA WFALLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDET HETMYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATP DTFEVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGF SIAKRTILLDASTLLSNNLSMFF C:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPGINTIRTWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP D:  PHFFKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEA WFALLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDET HETMYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATP DTFEVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGF SIAKRTILLDASTLLSNNLSMFF E:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPGINTIRTWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP F:  SPHFFKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYE AWFALLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDE THETMYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETAT PDTFEVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLG FSIAKRTILLDASTLLSNNLSMFF G:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPGINTIRTWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP H:  FFKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWF ALLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHE TMYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDT FEVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSI AKRTILLDASTLLSNNLSMFF I:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPGINTIRTWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP J:  WPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFALLDKD IHYFMPLRTNRMIREGELEYSGDQDLAHFDETHETMYGRI RKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTFEVNSA FILYRNRLERQVDIFAGERRDVLRRADNNLGFSIAKRTIL LDASTLLSNNLSMFF K:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPGINTIRTWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP L:  HFFKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAW FALLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETH ETMYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPD TFEVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFS IAKRTILLDASTLLSNNLSMFF M:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPGINTIRTWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP N:  PHFFKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEA WFALLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDET HETMYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATP DTFEVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGF SIAKRTILLDASTLLSNNLSMFF O:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPGINTIRTWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP P:  FFKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWF ALLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHE TMYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDT FEVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSI AKRTILLDASTLLSNNLSMFF Q:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPGINTIRTWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP R:  FFKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWF ALLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHE TMYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDT FEVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSI AKRTILLDASTLLSNNLSMFF S:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPGINTIRTWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP T:  HFFKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAW FALLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETH ETMYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPD TFEVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFS IAKRTILLDASTLLSNNLSMFF U:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEFDKAEWGPLQARVATYKGLVFANWDVQAPDLETYLG DARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQFC SDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFRAA WGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAEQR LGHTGMPVRRMVGQHMTIFPTCSFLPGINTIRTWHPRGPN EIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQDD GENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFPGN VGYVYAEEAARGMYHHWMRMMSEPSWATLK V:  FFKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWF ALLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHE TMYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDT FEVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSI AKRTILLDASTLLSNNLSMFF W:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFDKAEWGPLQARVATYKGLVFANWDVQAPDLETYL GDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQF CSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFRA AWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAEQ RLGHTGMPVRRMVGQHMTIFPTCSFLPGINTIRTWHPRGP NEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQD DGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFPG NVGYVYAEEAARGMYHHWMRMMSEPSWATLKP X:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF Description Functional site 1) chain A residue 100 type sequence C description BINDING SITE FOR RESIDUE FES A 460 source : AC1 2) chain A residue 102 type sequence H description BINDING SITE FOR RESIDUE FES A 460 source : AC1 3) chain A residue 103 type sequence R description BINDING SITE FOR RESIDUE FES A 460 source : AC1 4) chain A residue 120 type sequence C description BINDING SITE FOR RESIDUE FES A 460 source : AC1 5) chain A residue 123 type sequence H description BINDING SITE FOR RESIDUE FES A 460 source : AC1 6) chain A residue 125 type sequence W description BINDING SITE FOR RESIDUE FES A 460 source : AC1 7) chain A residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 A 461 source : AC2 8) chain A residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 A 461 source : AC2 9) chain A residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 A 461 source : AC2 10) chain A residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 A 461 source : AC2 11) chain C residue 100 type sequence C description BINDING SITE FOR RESIDUE FES C 460 source : AC3 12) chain C residue 102 type sequence H description BINDING SITE FOR RESIDUE FES C 460 source : AC3 13) chain C residue 103 type sequence R description BINDING SITE FOR RESIDUE FES C 460 source : AC3 14) chain C residue 120 type sequence C description BINDING SITE FOR RESIDUE FES C 460 source : AC3 15) chain C residue 123 type sequence H description BINDING SITE FOR RESIDUE FES C 460 source : AC3 16) chain C residue 125 type sequence W description BINDING SITE FOR RESIDUE FES C 460 source : AC3 17) chain C residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 C 461 source : AC4 18) chain C residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 C 461 source : AC4 19) chain C residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 C 461 source : AC4 20) chain C residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 C 461 source : AC4 21) chain C residue 226 type sequence Q description BINDING SITE FOR RESIDUE BNL C 462 source : AC5 22) chain C residue 230 type sequence D description BINDING SITE FOR RESIDUE BNL C 462 source : AC5 23) chain C residue 231 type sequence M description BINDING SITE FOR RESIDUE BNL C 462 source : AC5 24) chain C residue 233 type sequence H description BINDING SITE FOR RESIDUE BNL C 462 source : AC5 25) chain C residue 323 type sequence H description BINDING SITE FOR RESIDUE BNL C 462 source : AC5 26) chain C residue 333 type sequence L description BINDING SITE FOR RESIDUE BNL C 462 source : AC5 27) chain E residue 100 type sequence C description BINDING SITE FOR RESIDUE FES E 460 source : AC6 28) chain E residue 102 type sequence H description BINDING SITE FOR RESIDUE FES E 460 source : AC6 29) chain E residue 103 type sequence R description BINDING SITE FOR RESIDUE FES E 460 source : AC6 30) chain E residue 120 type sequence C description BINDING SITE FOR RESIDUE FES E 460 source : AC6 31) chain E residue 123 type sequence H description BINDING SITE FOR RESIDUE FES E 460 source : AC6 32) chain E residue 125 type sequence W description BINDING SITE FOR RESIDUE FES E 460 source : AC6 33) chain E residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 E 461 source : AC7 34) chain E residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 E 461 source : AC7 35) chain E residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 E 461 source : AC7 36) chain E residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 E 461 source : AC7 37) chain E residue 226 type sequence Q description BINDING SITE FOR RESIDUE BNL E 462 source : AC8 38) chain E residue 230 type sequence D description BINDING SITE FOR RESIDUE BNL E 462 source : AC8 39) chain E residue 231 type sequence M description BINDING SITE FOR RESIDUE BNL E 462 source : AC8 40) chain E residue 233 type sequence H description BINDING SITE FOR RESIDUE BNL E 462 source : AC8 41) chain E residue 323 type sequence H description BINDING SITE FOR RESIDUE BNL E 462 source : AC8 42) chain E residue 333 type sequence L description BINDING SITE FOR RESIDUE BNL E 462 source : AC8 43) chain G residue 100 type sequence C description BINDING SITE FOR RESIDUE FES G 460 source : AC9 44) chain G residue 102 type sequence H description BINDING SITE FOR RESIDUE FES G 460 source : AC9 45) chain G residue 103 type sequence R description BINDING SITE FOR RESIDUE FES G 460 source : AC9 46) chain G residue 120 type sequence C description BINDING SITE FOR RESIDUE FES G 460 source : AC9 47) chain G residue 123 type sequence H description BINDING SITE FOR RESIDUE FES G 460 source : AC9 48) chain G residue 125 type sequence W description BINDING SITE FOR RESIDUE FES G 460 source : AC9 49) chain G residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 G 461 source : BC1 50) chain G residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 G 461 source : BC1 51) chain G residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 G 461 source : BC1 52) chain G residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 G 461 source : BC1 53) chain I residue 100 type sequence C description BINDING SITE FOR RESIDUE FES I 460 source : BC2 54) chain I residue 102 type sequence H description BINDING SITE FOR RESIDUE FES I 460 source : BC2 55) chain I residue 103 type sequence R description BINDING SITE FOR RESIDUE FES I 460 source : BC2 56) chain I residue 105 type sequence M description BINDING SITE FOR RESIDUE FES I 460 source : BC2 57) chain I residue 120 type sequence C description BINDING SITE FOR RESIDUE FES I 460 source : BC2 58) chain I residue 123 type sequence H description BINDING SITE FOR RESIDUE FES I 460 source : BC2 59) chain I residue 125 type sequence W description BINDING SITE FOR RESIDUE FES I 460 source : BC2 60) chain I residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 I 461 source : BC3 61) chain I residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 I 461 source : BC3 62) chain I residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 I 461 source : BC3 63) chain I residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 I 461 source : BC3 64) chain I residue 226 type sequence Q description BINDING SITE FOR RESIDUE BNL I 462 source : BC4 65) chain I residue 230 type sequence D description BINDING SITE FOR RESIDUE BNL I 462 source : BC4 66) chain I residue 233 type sequence H description BINDING SITE FOR RESIDUE BNL I 462 source : BC4 67) chain I residue 323 type sequence H description BINDING SITE FOR RESIDUE BNL I 462 source : BC4 68) chain I residue 333 type sequence L description BINDING SITE FOR RESIDUE BNL I 462 source : BC4 69) chain K residue 100 type sequence C description BINDING SITE FOR RESIDUE FES K 460 source : BC5 70) chain K residue 102 type sequence H description BINDING SITE FOR RESIDUE FES K 460 source : BC5 71) chain K residue 103 type sequence R description BINDING SITE FOR RESIDUE FES K 460 source : BC5 72) chain K residue 105 type sequence M description BINDING SITE FOR RESIDUE FES K 460 source : BC5 73) chain K residue 120 type sequence C description BINDING SITE FOR RESIDUE FES K 460 source : BC5 74) chain K residue 123 type sequence H description BINDING SITE FOR RESIDUE FES K 460 source : BC5 75) chain K residue 125 type sequence W description BINDING SITE FOR RESIDUE FES K 460 source : BC5 76) chain K residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 K 461 source : BC6 77) chain K residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 K 461 source : BC6 78) chain K residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 K 461 source : BC6 79) chain K residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 K 461 source : BC6 80) chain K residue 226 type sequence Q description BINDING SITE FOR RESIDUE BNL K 462 source : BC7 81) chain K residue 230 type sequence D description BINDING SITE FOR RESIDUE BNL K 462 source : BC7 82) chain K residue 233 type sequence H description BINDING SITE FOR RESIDUE BNL K 462 source : BC7 83) chain K residue 323 type sequence H description BINDING SITE FOR RESIDUE BNL K 462 source : BC7 84) chain K residue 333 type sequence L description BINDING SITE FOR RESIDUE BNL K 462 source : BC7 85) chain K residue 384 type sequence F description BINDING SITE FOR RESIDUE BNL K 462 source : BC7 86) chain M residue 100 type sequence C description BINDING SITE FOR RESIDUE FES M 460 source : BC8 87) chain M residue 102 type sequence H description BINDING SITE FOR RESIDUE FES M 460 source : BC8 88) chain M residue 103 type sequence R description BINDING SITE FOR RESIDUE FES M 460 source : BC8 89) chain M residue 120 type sequence C description BINDING SITE FOR RESIDUE FES M 460 source : BC8 90) chain M residue 123 type sequence H description BINDING SITE FOR RESIDUE FES M 460 source : BC8 91) chain M residue 125 type sequence W description BINDING SITE FOR RESIDUE FES M 460 source : BC8 92) chain M residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 M 461 source : BC9 93) chain M residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 M 461 source : BC9 94) chain M residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 M 461 source : BC9 95) chain M residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 M 461 source : BC9 96) chain M residue 226 type sequence Q description BINDING SITE FOR RESIDUE BNL M 462 source : CC1 97) chain M residue 230 type sequence D description BINDING SITE FOR RESIDUE BNL M 462 source : CC1 98) chain M residue 233 type sequence H description BINDING SITE FOR RESIDUE BNL M 462 source : CC1 99) chain M residue 323 type sequence H description BINDING SITE FOR RESIDUE BNL M 462 source : CC1 100) chain M residue 333 type sequence L description BINDING SITE FOR RESIDUE BNL M 462 source : CC1 101) chain M residue 378 type sequence F description BINDING SITE FOR RESIDUE BNL M 462 source : CC1 102) chain M residue 384 type sequence F description BINDING SITE FOR RESIDUE BNL M 462 source : CC1 103) chain O residue 100 type sequence C description BINDING SITE FOR RESIDUE FES O 460 source : CC2 104) chain O residue 102 type sequence H description BINDING SITE FOR RESIDUE FES O 460 source : CC2 105) chain O residue 103 type sequence R description BINDING SITE FOR RESIDUE FES O 460 source : CC2 106) chain O residue 120 type sequence C description BINDING SITE FOR RESIDUE FES O 460 source : CC2 107) chain O residue 123 type sequence H description BINDING SITE FOR RESIDUE FES O 460 source : CC2 108) chain O residue 125 type sequence W description BINDING SITE FOR RESIDUE FES O 460 source : CC2 109) chain O residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 O 461 source : CC3 110) chain O residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 O 461 source : CC3 111) chain O residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 O 461 source : CC3 112) chain O residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 O 461 source : CC3 113) chain O residue 226 type sequence Q description BINDING SITE FOR RESIDUE BNL O 462 source : CC4 114) chain O residue 230 type sequence D description BINDING SITE FOR RESIDUE BNL O 462 source : CC4 115) chain O residue 233 type sequence H description BINDING SITE FOR RESIDUE BNL O 462 source : CC4 116) chain O residue 323 type sequence H description BINDING SITE FOR RESIDUE BNL O 462 source : CC4 117) chain O residue 333 type sequence L description BINDING SITE FOR RESIDUE BNL O 462 source : CC4 118) chain O residue 384 type sequence F description BINDING SITE FOR RESIDUE BNL O 462 source : CC4 119) chain Q residue 100 type sequence C description BINDING SITE FOR RESIDUE FES Q 460 source : CC5 120) chain Q residue 102 type sequence H description BINDING SITE FOR RESIDUE FES Q 460 source : CC5 121) chain Q residue 120 type sequence C description BINDING SITE FOR RESIDUE FES Q 460 source : CC5 122) chain Q residue 123 type sequence H description BINDING SITE FOR RESIDUE FES Q 460 source : CC5 123) chain Q residue 125 type sequence W description BINDING SITE FOR RESIDUE FES Q 460 source : CC5 124) chain Q residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 Q 461 source : CC6 125) chain Q residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 Q 461 source : CC6 126) chain Q residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 Q 461 source : CC6 127) chain Q residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 Q 461 source : CC6 128) chain Q residue 226 type sequence Q description BINDING SITE FOR RESIDUE BNL Q 462 source : CC7 129) chain Q residue 230 type sequence D description BINDING SITE FOR RESIDUE BNL Q 462 source : CC7 130) chain Q residue 233 type sequence H description BINDING SITE FOR RESIDUE BNL Q 462 source : CC7 131) chain Q residue 321 type sequence G description BINDING SITE FOR RESIDUE BNL Q 462 source : CC7 132) chain Q residue 323 type sequence H description BINDING SITE FOR RESIDUE BNL Q 462 source : CC7 133) chain Q residue 333 type sequence L description BINDING SITE FOR RESIDUE BNL Q 462 source : CC7 134) chain S residue 100 type sequence C description BINDING SITE FOR RESIDUE FES S 460 source : CC8 135) chain S residue 102 type sequence H description BINDING SITE FOR RESIDUE FES S 460 source : CC8 136) chain S residue 103 type sequence R description BINDING SITE FOR RESIDUE FES S 460 source : CC8 137) chain S residue 120 type sequence C description BINDING SITE FOR RESIDUE FES S 460 source : CC8 138) chain S residue 122 type sequence Y description BINDING SITE FOR RESIDUE FES S 460 source : CC8 139) chain S residue 123 type sequence H description BINDING SITE FOR RESIDUE FES S 460 source : CC8 140) chain S residue 125 type sequence W description BINDING SITE FOR RESIDUE FES S 460 source : CC8 141) chain S residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 S 461 source : CC9 142) chain S residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 S 461 source : CC9 143) chain S residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 S 461 source : CC9 144) chain S residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 S 461 source : CC9 145) chain S residue 226 type sequence Q description BINDING SITE FOR RESIDUE BNL S 462 source : DC1 146) chain S residue 230 type sequence D description BINDING SITE FOR RESIDUE BNL S 462 source : DC1 147) chain S residue 231 type sequence M description BINDING SITE FOR RESIDUE BNL S 462 source : DC1 148) chain S residue 233 type sequence H description BINDING SITE FOR RESIDUE BNL S 462 source : DC1 149) chain S residue 323 type sequence H description BINDING SITE FOR RESIDUE BNL S 462 source : DC1 150) chain S residue 333 type sequence L description BINDING SITE FOR RESIDUE BNL S 462 source : DC1 151) chain S residue 384 type sequence F description BINDING SITE FOR RESIDUE BNL S 462 source : DC1 152) chain U residue 100 type sequence C description BINDING SITE FOR RESIDUE FES U 460 source : DC2 153) chain U residue 102 type sequence H description BINDING SITE FOR RESIDUE FES U 460 source : DC2 154) chain U residue 103 type sequence R description BINDING SITE FOR RESIDUE FES U 460 source : DC2 155) chain U residue 120 type sequence C description BINDING SITE FOR RESIDUE FES U 460 source : DC2 156) chain U residue 122 type sequence Y description BINDING SITE FOR RESIDUE FES U 460 source : DC2 157) chain U residue 123 type sequence H description BINDING SITE FOR RESIDUE FES U 460 source : DC2 158) chain U residue 125 type sequence W description BINDING SITE FOR RESIDUE FES U 460 source : DC2 159) chain U residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 U 461 source : DC3 160) chain U residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 U 461 source : DC3 161) chain U residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 U 461 source : DC3 162) chain U residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 U 461 source : DC3 163) chain W residue 100 type sequence C description BINDING SITE FOR RESIDUE FES W 460 source : DC4 164) chain W residue 102 type sequence H description BINDING SITE FOR RESIDUE FES W 460 source : DC4 165) chain W residue 103 type sequence R description BINDING SITE FOR RESIDUE FES W 460 source : DC4 166) chain W residue 120 type sequence C description BINDING SITE FOR RESIDUE FES W 460 source : DC4 167) chain W residue 122 type sequence Y description BINDING SITE FOR RESIDUE FES W 460 source : DC4 168) chain W residue 123 type sequence H description BINDING SITE FOR RESIDUE FES W 460 source : DC4 169) chain W residue 125 type sequence W description BINDING SITE FOR RESIDUE FES W 460 source : DC4 170) chain W residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 W 461 source : DC5 171) chain W residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 W 461 source : DC5 172) chain W residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 W 461 source : DC5 173) chain W residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 W 461 source : DC5 174) chain W residue 226 type sequence Q description BINDING SITE FOR RESIDUE BNL W 462 source : DC6 175) chain W residue 230 type sequence D description BINDING SITE FOR RESIDUE BNL W 462 source : DC6 176) chain W residue 233 type sequence H description BINDING SITE FOR RESIDUE BNL W 462 source : DC6 177) chain W residue 323 type sequence H description BINDING SITE FOR RESIDUE BNL W 462 source : DC6 178) chain W residue 333 type sequence L description BINDING SITE FOR RESIDUE BNL W 462 source : DC6 179) chain A residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 180) chain E residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 181) chain E residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 182) chain E residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 183) chain G residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 184) chain G residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 185) chain G residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 186) chain G residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 187) chain I residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 188) chain I residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 189) chain I residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 190) chain A residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 191) chain I residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 192) chain K residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 193) chain K residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 194) chain K residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 195) chain K residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 196) chain M residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 197) chain M residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 198) chain M residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 199) chain M residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 200) chain O residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 201) chain A residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 202) chain O residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 203) chain O residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 204) chain O residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 205) chain Q residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 206) chain Q residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 207) chain Q residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 208) chain Q residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 209) chain S residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 210) chain S residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 211) chain S residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 212) chain A residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 213) chain S residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 214) chain U residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 215) chain U residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 216) chain U residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 217) chain U residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 218) chain W residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 219) chain W residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 220) chain W residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 221) chain W residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 222) chain C residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 223) chain C residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 224) chain C residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 225) chain C residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 226) chain E residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 227) chain A residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 228) chain I residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 229) chain K residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 230) chain K residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 231) chain M residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 232) chain M residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 233) chain O residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 234) chain O residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 235) chain Q residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 236) chain Q residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 237) chain S residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 238) chain A residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 239) chain S residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 240) chain U residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 241) chain U residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 242) chain W residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 243) chain W residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 244) chain C residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 245) chain C residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 246) chain E residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 247) chain E residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 248) chain G residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 249) chain G residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 250) chain I residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 251) chain A residue 100-123 type prosite sequence CRHRGMRICRSDAGNAKAFTCSYH description RING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CrHRGmricrsdaGNakaftCsYH source prosite : PS00570

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