eF-site ID 2xsh-ABCDEF PDB Code 2xsh Chain A, B, C, D, E, F 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 A:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPAMNNIRIWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP B:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF C:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPAMNNIRIWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP D:  FKTFEWPSKAAGLELQNEIEQFYYREAQLLDHRAYEAWFA LLDKDIHYFMPLRTNRMIREGELEYSGDQDLAHFDETHET MYGRIRKVTSDVGWAENPPSRTRHLVSNVIVKETATPDTF EVNSAFILYRNRLERQVDIFAGERRDVLRRADNNLGFSIA KRTILLDASTLLSNNLSMFF E:  NWTPEAIRGLVDQEKGLLDPRIYADQSLYELELERVFGRS WLLLGHESHVPETGDFLATYMGEDPVVMVRQKDKSIKVFL NQCRHRGMRICRSDAGNAKAFTCSYHGWAYDIAGKLVNVP FEKEAFFDKAEWGPLQARVATYKGLVFANWDVQAPDLETY LGDARPYMDVMLDRTPAGTVAIGGMQKWVIPCNWKFAAEQ FCSDMYHAGTTTHLSGILAGIPPEMDLSQAQIPTKGNQFR AAWGGHGSGWYVDEPGSLLAVMGPKVTQYWTEGPAAELAE QRLGHTGMPVRRMVGQHMTIFPTCSFLPAMNNIRIWHPRG PNEIEVWAFTLVDADAPAEIKEEYRRHNIRNFSAGGVFEQ DDGENWVEIQKGLRGYKAKSQPLNAQMGLGRSQTGHPDFP GNVGYVYAEEAARGMYHHWMRMMSEPSWATLKP F:  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 DC5 A 902 source : AC3 12) chain A residue 230 type sequence D description BINDING SITE FOR RESIDUE DC5 A 902 source : AC3 13) chain A residue 231 type sequence M description BINDING SITE FOR RESIDUE DC5 A 902 source : AC3 14) chain A residue 233 type sequence H description BINDING SITE FOR RESIDUE DC5 A 902 source : AC3 15) chain A residue 239 type sequence H description BINDING SITE FOR RESIDUE DC5 A 902 source : AC3 16) chain A residue 283 type sequence S description BINDING SITE FOR RESIDUE DC5 A 902 source : AC3 17) chain A residue 322 type sequence Q description BINDING SITE FOR RESIDUE DC5 A 902 source : AC3 18) chain A residue 323 type sequence H description BINDING SITE FOR RESIDUE DC5 A 902 source : AC3 19) chain A residue 333 type sequence L description BINDING SITE FOR RESIDUE DC5 A 902 source : AC3 20) chain A residue 384 type sequence F description BINDING SITE FOR RESIDUE DC5 A 902 source : AC3 21) chain C residue 100 type sequence C description BINDING SITE FOR RESIDUE FES C 900 source : AC4 22) chain C residue 102 type sequence H description BINDING SITE FOR RESIDUE FES C 900 source : AC4 23) chain C residue 103 type sequence R description BINDING SITE FOR RESIDUE FES C 900 source : AC4 24) chain C residue 120 type sequence C description BINDING SITE FOR RESIDUE FES C 900 source : AC4 25) chain C residue 123 type sequence H description BINDING SITE FOR RESIDUE FES C 900 source : AC4 26) chain C residue 125 type sequence W description BINDING SITE FOR RESIDUE FES C 900 source : AC4 27) chain C residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 C 901 source : AC5 28) chain C residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 C 901 source : AC5 29) chain C residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 C 901 source : AC5 30) chain C residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 C 901 source : AC5 31) chain C residue 226 type sequence Q description BINDING SITE FOR RESIDUE DC5 C 902 source : AC6 32) chain C residue 230 type sequence D description BINDING SITE FOR RESIDUE DC5 C 902 source : AC6 33) chain C residue 231 type sequence M description BINDING SITE FOR RESIDUE DC5 C 902 source : AC6 34) chain C residue 233 type sequence H description BINDING SITE FOR RESIDUE DC5 C 902 source : AC6 35) chain C residue 234 type sequence A description BINDING SITE FOR RESIDUE DC5 C 902 source : AC6 36) chain C residue 239 type sequence H description BINDING SITE FOR RESIDUE DC5 C 902 source : AC6 37) chain C residue 322 type sequence Q description BINDING SITE FOR RESIDUE DC5 C 902 source : AC6 38) chain C residue 323 type sequence H description BINDING SITE FOR RESIDUE DC5 C 902 source : AC6 39) chain C residue 333 type sequence L description BINDING SITE FOR RESIDUE DC5 C 902 source : AC6 40) chain C residue 384 type sequence F description BINDING SITE FOR RESIDUE DC5 C 902 source : AC6 41) chain E residue 226 type sequence Q description BINDING SITE FOR RESIDUE DC5 E 900 source : AC7 42) chain E residue 230 type sequence D description BINDING SITE FOR RESIDUE DC5 E 900 source : AC7 43) chain E residue 231 type sequence M description BINDING SITE FOR RESIDUE DC5 E 900 source : AC7 44) chain E residue 233 type sequence H description BINDING SITE FOR RESIDUE DC5 E 900 source : AC7 45) chain E residue 234 type sequence A description BINDING SITE FOR RESIDUE DC5 E 900 source : AC7 46) chain E residue 239 type sequence H description BINDING SITE FOR RESIDUE DC5 E 900 source : AC7 47) chain E residue 322 type sequence Q description BINDING SITE FOR RESIDUE DC5 E 900 source : AC7 48) chain E residue 323 type sequence H description BINDING SITE FOR RESIDUE DC5 E 900 source : AC7 49) chain E residue 333 type sequence L description BINDING SITE FOR RESIDUE DC5 E 900 source : AC7 50) chain E residue 336 type sequence M description BINDING SITE FOR RESIDUE DC5 E 900 source : AC7 51) chain E residue 384 type sequence F description BINDING SITE FOR RESIDUE DC5 E 900 source : AC7 52) chain E residue 100 type sequence C description BINDING SITE FOR RESIDUE FES E 901 source : AC8 53) chain E residue 102 type sequence H description BINDING SITE FOR RESIDUE FES E 901 source : AC8 54) chain E residue 103 type sequence R description BINDING SITE FOR RESIDUE FES E 901 source : AC8 55) chain E residue 105 type sequence M description BINDING SITE FOR RESIDUE FES E 901 source : AC8 56) chain E residue 120 type sequence C description BINDING SITE FOR RESIDUE FES E 901 source : AC8 57) chain E residue 123 type sequence H description BINDING SITE FOR RESIDUE FES E 901 source : AC8 58) chain E residue 125 type sequence W description BINDING SITE FOR RESIDUE FES E 901 source : AC8 59) chain E residue 226 type sequence Q description BINDING SITE FOR RESIDUE FE2 E 902 source : AC9 60) chain E residue 233 type sequence H description BINDING SITE FOR RESIDUE FE2 E 902 source : AC9 61) chain E residue 239 type sequence H description BINDING SITE FOR RESIDUE FE2 E 902 source : AC9 62) chain E residue 388 type sequence D description BINDING SITE FOR RESIDUE FE2 E 902 source : AC9 63) chain A residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 64) chain E residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 65) chain E residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 66) chain E residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 67) chain A residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 68) chain A residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 69) chain A residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 70) chain C residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 71) chain C residue 102 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 72) chain C residue 120 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 73) chain C residue 123 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 74) chain E residue 100 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628 source Swiss-Prot : SWS_FT_FI1 75) chain A residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 76) chain A residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 77) chain C residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 78) chain C residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 79) chain E residue 233 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 80) chain E residue 239 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 81) chain A residue 100-123 type prosite sequence CRHRGMRICRSDAGNAKAFTCSYH description RING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CrHRGmricrsdaGNakaftCsYH source prosite : PS00570

Display surface Download Links