eF-site ID 5aeu-ABCDEFGH PDB Code 5aeu Chain A, B, C, D, E, F, G, H click to enlarge Title Crystal structure of II9 variant of Biphenyl dioxygenase from Burkholderia xenovorans LB400 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:  HFFKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAW FALLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETH ETMYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPD TFEVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFS IAKRTILLDASTLLSNNLSMFF E:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPGINTIRTWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP F:  HFFKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAW FALLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETH ETMYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPD TFEVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFS IAKRTILLDASTLLSNNLSMFF G:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPGINTIRTWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP H:  HFFKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAW FALLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETH ETMYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPD TFEVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFS IAKRTILLDASTLLSNNLSMFF Description Functional site 1) chain A residue 100 type sequence C description BINDING SITE FOR RESIDUE FES A 500 source : AC1 2) chain A residue 102 type sequence H description BINDING SITE FOR RESIDUE FES A 500 source : AC1 3) chain A residue 103 type sequence R description BINDING SITE FOR RESIDUE FES A 500 source : AC1 4) chain A residue 120 type sequence C description BINDING SITE FOR RESIDUE FES A 500 source : AC1 5) chain A residue 123 type sequence H description BINDING SITE FOR RESIDUE FES A 500 source : AC1 6) chain A residue 125 type sequence W description BINDING SITE FOR RESIDUE FES A 500 source : AC1 7) chain A residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 A 501 source : AC2 8) chain A residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 A 501 source : AC2 9) chain A residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 A 501 source : AC2 10) chain A residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 A 501 source : AC2 11) chain C residue 100 type sequence C description BINDING SITE FOR RESIDUE FES C 500 source : AC3 12) chain C residue 102 type sequence H description BINDING SITE FOR RESIDUE FES C 500 source : AC3 13) chain C residue 103 type sequence R description BINDING SITE FOR RESIDUE FES C 500 source : AC3 14) chain C residue 120 type sequence C description BINDING SITE FOR RESIDUE FES C 500 source : AC3 15) chain C residue 123 type sequence H description BINDING SITE FOR RESIDUE FES C 500 source : AC3 16) chain C residue 124 type sequence G description BINDING SITE FOR RESIDUE FES C 500 source : AC3 17) chain C residue 125 type sequence W description BINDING SITE FOR RESIDUE FES C 500 source : AC3 18) chain C residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 C 501 source : AC4 19) chain C residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 C 501 source : AC4 20) chain C residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 C 501 source : AC4 21) chain C residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 C 501 source : AC4 22) chain E residue 100 type sequence C description BINDING SITE FOR RESIDUE FES E 500 source : AC5 23) chain E residue 102 type sequence H description BINDING SITE FOR RESIDUE FES E 500 source : AC5 24) chain E residue 103 type sequence R description BINDING SITE FOR RESIDUE FES E 500 source : AC5 25) chain E residue 120 type sequence C description BINDING SITE FOR RESIDUE FES E 500 source : AC5 26) chain E residue 122 type sequence Y description BINDING SITE FOR RESIDUE FES E 500 source : AC5 27) chain E residue 123 type sequence H description BINDING SITE FOR RESIDUE FES E 500 source : AC5 28) chain E residue 125 type sequence W description BINDING SITE FOR RESIDUE FES E 500 source : AC5 29) chain E residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 E 501 source : AC6 30) chain E residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 E 501 source : AC6 31) chain E residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 E 501 source : AC6 32) chain E residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 E 501 source : AC6 33) chain G residue 100 type sequence C description BINDING SITE FOR RESIDUE FES G 500 source : AC7 34) chain G residue 102 type sequence H description BINDING SITE FOR RESIDUE FES G 500 source : AC7 35) chain G residue 103 type sequence R description BINDING SITE FOR RESIDUE FES G 500 source : AC7 36) chain G residue 120 type sequence C description BINDING SITE FOR RESIDUE FES G 500 source : AC7 37) chain G residue 123 type sequence H description BINDING SITE FOR RESIDUE FES G 500 source : AC7 38) chain G residue 125 type sequence W description BINDING SITE FOR RESIDUE FES G 500 source : AC7 39) chain G residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 G 501 source : AC8 40) chain G residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 G 501 source : AC8 41) chain G residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 G 501 source : AC8 42) chain G residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 G 501 source : AC8 43) chain A residue 100-123 type prosite sequence CRHRGMRICRSDAGNAKAFTCSYH description RING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CrHRGmricrsdaGNakaftCsYH source prosite : PS00570 44) chain A residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 45) chain E residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 46) chain E residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 47) chain E residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 48) chain G residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 49) chain G residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 50) chain G residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 51) chain G residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 52) chain A residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 53) chain A residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 54) chain A residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 55) chain C residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 56) chain C residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 57) chain C residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 58) chain C residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 59) chain E residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 60) chain A residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 61) chain A residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 62) chain C residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 63) chain C residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 64) chain E residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 65) chain E residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 66) chain G residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 67) chain G residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2

Display surface Download Links