eF-site ID 1mpy-ABCD PDB Code 1mpy Chain A, B, C, D click to enlarge Title STRUCTURE OF CATECHOL 2,3-DIOXYGENASE (METAPYROCATECHASE) FROM PSEUDOMONAS PUTIDA MT-2 Classification OXIDOREDUCTASE Compound CATECHOL 2,3-DIOXYGENASE Source Pseudomonas putida (Arthrobacter siderocapsulatus) (XYLE1_PSEPU) Sequence A:  MNKGVMRPGHVQLRVLDMSKALEHYVELLGLIEMDRDDQG RVYLKAWTEVDKFSLVLREADEPGMDFMGFKVVDEDALRQ LERDLMAYGCAVEQLPAGELNSCGRRVRFQAPSGHHFELY ADKEYTGKWGLNDVNPEAWPRDLKGMAAVRFDHALMYGDE LPATYDLFTKVLGFYLAEQVLDENGTRVAQFLSLSTKAHD VAFIHHPEKGRLHHVSFHLETWEDLLRAADLISMTDTSID IGPTRHGLTHGKTIYFFDPSGNRNEVFCGGDYNYPDHKPV TWTTDQLGKAIFYHDRILNERFMTVLT B:  MNKGVMRPGHVQLRVLDMSKALEHYVELLGLIEMDRDDQG RVYLKAWTEVDKFSLVLREADEPGMDFMGFKVVDEDALRQ LERDLMAYGCAVEQLPAGELNSCGRRVRFQAPSGHHFELY ADKEYTGKWGLNDVNPEAWPRDLKGMAAVRFDHALMYGDE LPATYDLFTKVLGFYLAEQVLDENGTRVAQFLSLSTKAHD VAFIHHPEKGRLHHVSFHLETWEDLLRAADLISMTDTSID IGPTRHGLTHGKTIYFFDPSGNRNEVFCGGDYNYPDHKPV TWTTDQLGKAIFYHDRILNERFMTVLT C:  MNKGVMRPGHVQLRVLDMSKALEHYVELLGLIEMDRDDQG RVYLKAWTEVDKFSLVLREADEPGMDFMGFKVVDEDALRQ LERDLMAYGCAVEQLPAGELNSCGRRVRFQAPSGHHFELY ADKEYTGKWGLNDVNPEAWPRDLKGMAAVRFDHALMYGDE LPATYDLFTKVLGFYLAEQVLDENGTRVAQFLSLSTKAHD VAFIHHPEKGRLHHVSFHLETWEDLLRAADLISMTDTSID IGPTRHGLTHGKTIYFFDPSGNRNEVFCGGDYNYPDHKPV TWTTDQLGKAIFYHDRILNERFMTVLT D:  MNKGVMRPGHVQLRVLDMSKALEHYVELLGLIEMDRDDQG RVYLKAWTEVDKFSLVLREADEPGMDFMGFKVVDEDALRQ LERDLMAYGCAVEQLPAGELNSCGRRVRFQAPSGHHFELY ADKEYTGKWGLNDVNPEAWPRDLKGMAAVRFDHALMYGDE LPATYDLFTKVLGFYLAEQVLDENGTRVAQFLSLSTKAHD VAFIHHPEKGRLHHVSFHLETWEDLLRAADLISMTDTSID IGPTRHGLTHGKTIYFFDPSGNRNEVFCGGDYNYPDHKPV TWTTDQLGKAIFYHDRILNERFMTVLT Description Functional site 1) chain A residue 153 type sequence H description BINDING SITE FOR RESIDUE FE2 A 308 source : AC1 2) chain A residue 214 type sequence H description BINDING SITE FOR RESIDUE FE2 A 308 source : AC1 3) chain A residue 216 type sequence S description BINDING SITE FOR RESIDUE FE2 A 308 source : AC1 4) chain A residue 265 type sequence E description BINDING SITE FOR RESIDUE FE2 A 308 source : AC1 5) chain B residue 153 type sequence H description BINDING SITE FOR RESIDUE FE2 B 308 source : AC2 6) chain B residue 214 type sequence H description BINDING SITE FOR RESIDUE FE2 B 308 source : AC2 7) chain B residue 216 type sequence S description BINDING SITE FOR RESIDUE FE2 B 308 source : AC2 8) chain B residue 255 type sequence Y description BINDING SITE FOR RESIDUE FE2 B 308 source : AC2 9) chain B residue 265 type sequence E description BINDING SITE FOR RESIDUE FE2 B 308 source : AC2 10) chain C residue 153 type sequence H description BINDING SITE FOR RESIDUE FE2 C 308 source : AC3 11) chain C residue 214 type sequence H description BINDING SITE FOR RESIDUE FE2 C 308 source : AC3 12) chain C residue 216 type sequence S description BINDING SITE FOR RESIDUE FE2 C 308 source : AC3 13) chain C residue 265 type sequence E description BINDING SITE FOR RESIDUE FE2 C 308 source : AC3 14) chain D residue 153 type sequence H description BINDING SITE FOR RESIDUE FE2 D 308 source : AC4 15) chain D residue 214 type sequence H description BINDING SITE FOR RESIDUE FE2 D 308 source : AC4 16) chain D residue 216 type sequence S description BINDING SITE FOR RESIDUE FE2 D 308 source : AC4 17) chain D residue 265 type sequence E description BINDING SITE FOR RESIDUE FE2 D 308 source : AC4 18) chain A residue 191 type sequence F description BINDING SITE FOR RESIDUE ACN A 309 source : AC5 19) chain A residue 246 type sequence H description BINDING SITE FOR RESIDUE ACN A 309 source : AC5 20) chain A residue 248 type sequence L description BINDING SITE FOR RESIDUE ACN A 309 source : AC5 21) chain A residue 249 type sequence T description BINDING SITE FOR RESIDUE ACN A 309 source : AC5 22) chain A residue 255 type sequence Y description BINDING SITE FOR RESIDUE ACN A 309 source : AC5 23) chain B residue 246 type sequence H description BINDING SITE FOR RESIDUE ACN B 309 source : AC6 24) chain B residue 248 type sequence L description BINDING SITE FOR RESIDUE ACN B 309 source : AC6 25) chain B residue 249 type sequence T description BINDING SITE FOR RESIDUE ACN B 309 source : AC6 26) chain B residue 255 type sequence Y description BINDING SITE FOR RESIDUE ACN B 309 source : AC6 27) chain C residue 246 type sequence H description BINDING SITE FOR RESIDUE ACN C 309 source : AC7 28) chain C residue 248 type sequence L description BINDING SITE FOR RESIDUE ACN C 309 source : AC7 29) chain C residue 255 type sequence Y description BINDING SITE FOR RESIDUE ACN C 309 source : AC7 30) chain D residue 155 type sequence L description BINDING SITE FOR RESIDUE ACN D 309 source : AC8 31) chain D residue 246 type sequence H description BINDING SITE FOR RESIDUE ACN D 309 source : AC8 32) chain D residue 255 type sequence Y description BINDING SITE FOR RESIDUE ACN D 309 source : AC8 33) chain D residue 291 type sequence I description BINDING SITE FOR RESIDUE ACN D 309 source : AC8 34) chain A residue 153 type catalytic sequence H description 34 source MCSA : MCSA1 35) chain A residue 199 type catalytic sequence H description 34 source MCSA : MCSA1 36) chain A residue 214 type catalytic sequence H description 34 source MCSA : MCSA1 37) chain A residue 246 type catalytic sequence H description 34 source MCSA : MCSA1 38) chain A residue 255 type catalytic sequence Y description 34 source MCSA : MCSA1 39) chain A residue 265 type catalytic sequence E description 34 source MCSA : MCSA1 40) chain B residue 153 type catalytic sequence H description 34 source MCSA : MCSA2 41) chain B residue 199 type catalytic sequence H description 34 source MCSA : MCSA2 42) chain B residue 214 type catalytic sequence H description 34 source MCSA : MCSA2 43) chain B residue 246 type catalytic sequence H description 34 source MCSA : MCSA2 44) chain B residue 255 type catalytic sequence Y description 34 source MCSA : MCSA2 45) chain B residue 265 type catalytic sequence E description 34 source MCSA : MCSA2 46) chain C residue 153 type catalytic sequence H description 34 source MCSA : MCSA3 47) chain C residue 199 type catalytic sequence H description 34 source MCSA : MCSA3 48) chain C residue 214 type catalytic sequence H description 34 source MCSA : MCSA3 49) chain C residue 246 type catalytic sequence H description 34 source MCSA : MCSA3 50) chain C residue 255 type catalytic sequence Y description 34 source MCSA : MCSA3 51) chain C residue 265 type catalytic sequence E description 34 source MCSA : MCSA3 52) chain D residue 153 type catalytic sequence H description 34 source MCSA : MCSA4 53) chain D residue 199 type catalytic sequence H description 34 source MCSA : MCSA4 54) chain D residue 214 type catalytic sequence H description 34 source MCSA : MCSA4 55) chain D residue 246 type catalytic sequence H description 34 source MCSA : MCSA4 56) chain D residue 255 type catalytic sequence Y description 34 source MCSA : MCSA4 57) chain D residue 265 type catalytic sequence E description 34 source MCSA : MCSA4 58) chain A residue 244-265 type prosite sequence TRHGLTHGKTIYFFDPSGNRNE description EXTRADIOL_DIOXYGENAS Extradiol ring-cleavage dioxygenases signature. TrHglthgktIYffDPsGnrnE source prosite : PS00082 59) chain A residue 153 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 60) chain D residue 153 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 61) chain D residue 214 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 62) chain D residue 265 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 63) chain A residue 214 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 64) chain A residue 265 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 65) chain B residue 153 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 66) chain B residue 214 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 67) chain B residue 265 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 68) chain C residue 153 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 69) chain C residue 214 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 70) chain C residue 265 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1

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