eF-site ID 2xsh-GHIJKL PDB Code 2xsh Chain G, H, I, J, K, L click to enlarge Title CRYSTAL STRUCTURE OF P4 VARIANT OF BIPHENYL DIOXYGENASE FROM BURKHOLDERIA XENOVORANS LB400 IN COMPLEX WITH 2,6 DI CHLOROBIPHENYL Classification OXIDOREDUCTASE Compound BIPHENYL DIOXYGENASE SUBUNIT ALPHA Source Burkholderia xenovorans (strain LB400) (BPHE_BURXL) Sequence G:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPAMNNIRIWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP H:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF I:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPAMNNIRIWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP J:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF K:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPAMNNIRIWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP L:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF Description Functional site 1) chain G residue 100 type sequence C description BINDING SITE FOR RESIDUE FES G 900 source : BC1 2) chain G residue 102 type sequence H description BINDING SITE FOR RESIDUE FES G 900 source : BC1 3) chain G residue 103 type sequence R description BINDING SITE FOR RESIDUE FES G 900 source : BC1 4) chain G residue 120 type sequence C description BINDING SITE FOR RESIDUE FES G 900 source : BC1 5) chain G residue 123 type sequence H description BINDING SITE FOR RESIDUE FES G 900 source : BC1 6) chain G residue 125 type sequence W description BINDING SITE FOR RESIDUE FES G 900 source : BC1 7) chain G residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 G 901 source : BC2 8) chain G residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 G 901 source : BC2 9) chain G residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 G 901 source : BC2 10) chain G residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 G 901 source : BC2 11) chain I residue 100 type sequence C description BINDING SITE FOR RESIDUE FES I 900 source : BC3 12) chain I residue 102 type sequence H description BINDING SITE FOR RESIDUE FES I 900 source : BC3 13) chain I residue 103 type sequence R description BINDING SITE FOR RESIDUE FES I 900 source : BC3 14) chain I residue 120 type sequence C description BINDING SITE FOR RESIDUE FES I 900 source : BC3 15) chain I residue 123 type sequence H description BINDING SITE FOR RESIDUE FES I 900 source : BC3 16) chain I residue 125 type sequence W description BINDING SITE FOR RESIDUE FES I 900 source : BC3 17) chain I residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 I 901 source : BC4 18) chain I residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 I 901 source : BC4 19) chain I residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 I 901 source : BC4 20) chain I residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 I 901 source : BC4 21) chain K residue 100 type sequence C description BINDING SITE FOR RESIDUE FES K 900 source : BC5 22) chain K residue 102 type sequence H description BINDING SITE FOR RESIDUE FES K 900 source : BC5 23) chain K residue 103 type sequence R description BINDING SITE FOR RESIDUE FES K 900 source : BC5 24) chain K residue 120 type sequence C description BINDING SITE FOR RESIDUE FES K 900 source : BC5 25) chain K residue 123 type sequence H description BINDING SITE FOR RESIDUE FES K 900 source : BC5 26) chain K residue 125 type sequence W description BINDING SITE FOR RESIDUE FES K 900 source : BC5 27) chain K residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 K 901 source : BC6 28) chain K residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 K 901 source : BC6 29) chain K residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 K 901 source : BC6 30) chain K residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 K 901 source : BC6 31) chain G residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 32) chain G residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 33) chain G residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 34) chain G residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 35) chain I residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 36) chain I residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 37) chain I residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 38) chain I residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 39) chain K residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 40) chain K residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 41) chain K residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 42) chain K residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 43) chain I residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 44) chain K residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 45) chain K residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 46) chain G residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 47) chain G residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 48) chain I residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2

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