eF-site ID 2yfl-ABCDEFGHIJKL PDB Code 2yfl Chain A, B, C, D, E, F, G, H, I, J, K, L click to enlarge Title Crystal Structure of Biphenyl dioxygenase variant RR41 with 2-chloro dibenzofuran Classification OXIDOREDUCTASE Compound BIPHENYL DIOXYGENASE SUBUNIT ALPHA Source Burkholderia xenovorans (strain LB400) (BPHE_BURXL) Sequence A:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPAMNQIRVWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPFNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP B:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF C:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPAMNQIRVWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPFNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP D:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF E:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPAMNQIRVWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPFNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP F:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF G:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPAMNQIRVWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPFNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP H:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF I:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPAMNQIRVWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPFNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP J:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF K:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPAMNQIRVWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPFNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP L:  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 A residue 226 type sequence Q description BINDING SITE FOR RESIDUE DC4 A 1460 source : AC3 12) chain A residue 230 type sequence D description BINDING SITE FOR RESIDUE DC4 A 1460 source : AC3 13) chain A residue 231 type sequence M description BINDING SITE FOR RESIDUE DC4 A 1460 source : AC3 14) chain A residue 233 type sequence H description BINDING SITE FOR RESIDUE DC4 A 1460 source : AC3 15) chain A residue 283 type sequence S description BINDING SITE FOR RESIDUE DC4 A 1460 source : AC3 16) chain A residue 323 type sequence H description BINDING SITE FOR RESIDUE DC4 A 1460 source : AC3 17) chain A residue 333 type sequence L description BINDING SITE FOR RESIDUE DC4 A 1460 source : AC3 18) chain C residue 100 type sequence C description BINDING SITE FOR RESIDUE FES C 900 source : AC4 19) chain C residue 102 type sequence H description BINDING SITE FOR RESIDUE FES C 900 source : AC4 20) chain C residue 103 type sequence R description BINDING SITE FOR RESIDUE FES C 900 source : AC4 21) chain C residue 120 type sequence C description BINDING SITE FOR RESIDUE FES C 900 source : AC4 22) chain C residue 123 type sequence H description BINDING SITE FOR RESIDUE FES C 900 source : AC4 23) chain C residue 125 type sequence W description BINDING SITE FOR RESIDUE FES C 900 source : AC4 24) chain C residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 C 901 source : AC5 25) chain C residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 C 901 source : AC5 26) chain C residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 C 901 source : AC5 27) chain C residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 C 901 source : AC5 28) chain C residue 226 type sequence Q description BINDING SITE FOR RESIDUE DC4 C 1460 source : AC6 29) chain C residue 227 type sequence F description BINDING SITE FOR RESIDUE DC4 C 1460 source : AC6 30) chain C residue 230 type sequence D description BINDING SITE FOR RESIDUE DC4 C 1460 source : AC6 31) chain C residue 231 type sequence M description BINDING SITE FOR RESIDUE DC4 C 1460 source : AC6 32) chain C residue 233 type sequence H description BINDING SITE FOR RESIDUE DC4 C 1460 source : AC6 33) chain C residue 323 type sequence H description BINDING SITE FOR RESIDUE DC4 C 1460 source : AC6 34) chain C residue 378 type sequence F description BINDING SITE FOR RESIDUE DC4 C 1460 source : AC6 35) chain C residue 384 type sequence F description BINDING SITE FOR RESIDUE DC4 C 1460 source : AC6 36) chain C residue 388 type sequence D description BINDING SITE FOR RESIDUE DC4 C 1460 source : AC6 37) chain E residue 100 type sequence C description BINDING SITE FOR RESIDUE FES E 900 source : AC7 38) chain E residue 102 type sequence H description BINDING SITE FOR RESIDUE FES E 900 source : AC7 39) chain E residue 103 type sequence R description BINDING SITE FOR RESIDUE FES E 900 source : AC7 40) chain E residue 105 type sequence M description BINDING SITE FOR RESIDUE FES E 900 source : AC7 41) chain E residue 120 type sequence C description BINDING SITE FOR RESIDUE FES E 900 source : AC7 42) chain E residue 123 type sequence H description BINDING SITE FOR RESIDUE FES E 900 source : AC7 43) chain E residue 125 type sequence W description BINDING SITE FOR RESIDUE FES E 900 source : AC7 44) chain E residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 E 901 source : AC8 45) chain E residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 E 901 source : AC8 46) chain E residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 E 901 source : AC8 47) chain E residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 E 901 source : AC8 48) chain G residue 100 type sequence C description BINDING SITE FOR RESIDUE FES G 900 source : AC9 49) chain G residue 102 type sequence H description BINDING SITE FOR RESIDUE FES G 900 source : AC9 50) chain G residue 103 type sequence R description BINDING SITE FOR RESIDUE FES G 900 source : AC9 51) chain G residue 120 type sequence C description BINDING SITE FOR RESIDUE FES G 900 source : AC9 52) chain G residue 123 type sequence H description BINDING SITE FOR RESIDUE FES G 900 source : AC9 53) chain G residue 125 type sequence W description BINDING SITE FOR RESIDUE FES G 900 source : AC9 54) chain G residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 G 901 source : BC1 55) chain G residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 G 901 source : BC1 56) chain G residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 G 901 source : BC1 57) chain G residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 G 901 source : BC1 58) chain I residue 100 type sequence C description BINDING SITE FOR RESIDUE FES I 900 source : BC2 59) chain I residue 102 type sequence H description BINDING SITE FOR RESIDUE FES I 900 source : BC2 60) chain I residue 103 type sequence R description BINDING SITE FOR RESIDUE FES I 900 source : BC2 61) chain I residue 120 type sequence C description BINDING SITE FOR RESIDUE FES I 900 source : BC2 62) chain I residue 123 type sequence H description BINDING SITE FOR RESIDUE FES I 900 source : BC2 63) chain I residue 125 type sequence W description BINDING SITE FOR RESIDUE FES I 900 source : BC2 64) chain I residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 I 901 source : BC3 65) chain I residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 I 901 source : BC3 66) chain I residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 I 901 source : BC3 67) chain I residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 I 901 source : BC3 68) chain K residue 100 type sequence C description BINDING SITE FOR RESIDUE FES K 900 source : BC4 69) chain K residue 102 type sequence H description BINDING SITE FOR RESIDUE FES K 900 source : BC4 70) chain K residue 103 type sequence R description BINDING SITE FOR RESIDUE FES K 900 source : BC4 71) chain K residue 120 type sequence C description BINDING SITE FOR RESIDUE FES K 900 source : BC4 72) chain K residue 123 type sequence H description BINDING SITE FOR RESIDUE FES K 900 source : BC4 73) chain K residue 124 type sequence G description BINDING SITE FOR RESIDUE FES K 900 source : BC4 74) chain K residue 125 type sequence W description BINDING SITE FOR RESIDUE FES K 900 source : BC4 75) chain K residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 K 901 source : BC5 76) chain K residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 K 901 source : BC5 77) chain K residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 K 901 source : BC5 78) chain K residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 K 901 source : BC5 79) chain A residue 100-123 type prosite sequence CRHRGMRICRSDAGNAKAFTCSYH description RING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CrHRGmricrsdaGNakaftCsYH source prosite : PS00570 80) chain A residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 81) chain E residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 82) chain E residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 83) chain E residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 84) chain G residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 85) chain G residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 86) chain G residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 87) chain G residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 88) chain I residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 89) chain I residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 90) chain I residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 91) chain A residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 92) chain I residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 93) chain K residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 94) chain K residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 95) chain K residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 96) chain K residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 97) chain A residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 98) chain A residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 99) chain C residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 100) chain C residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 101) chain C residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 102) chain C residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 103) chain E residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 104) chain A residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 105) chain I residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 106) chain K residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 107) chain K residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 108) chain A residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 109) chain C residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 110) chain C residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 111) chain E residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 112) chain E residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 113) chain G residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 114) chain G residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 115) chain I residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2

Display surface Download Links