eF-site ID 1ykk-ABCDEFGHIJKL PDB Code 1ykk Chain A, B, C, D, E, F, G, H, I, J, K, L click to enlarge Title Protocatechuate 3,4-Dioxygenase Y408C Mutant Classification OXIDOREDUCTASE Compound Protocatechuate 3,4-dioxygenase alpha chain Source Pseudomonas putida (Arthrobacter siderocapsulatus) (PCXB_PSEPU) Sequence A:  PIELLPETPSQTAGPYVHIGLALEAAGNPTRDQEIWNRLA KPDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEYQ DAYNLENAFNSFGRTATTFDAGEWTLHTVKPGVVNNAAGV PMAPHINISLFARGINIHLHTRLYFDDEAQANAKCPVLNL IEQPQRRETLIAKRCEVDGKTAYRFDIRIQGEGETVFFDF B:  PAQDNSRFVIRDRNWHPKALTPDYKTSIARSPRQALVSIP QSISETTGPNFSHLGFGAHDHDLLLNFNNGGLPIGERIIV AGRVVDQYGKPVPNTLVEMWQANAGGRCRHKNDRYLAPLD PNFGGVGRXLTDSDGYYSFRTIKPGPYPWRNGPNDWRPAH IHFGISGPSIATKLITQLYFEGDPLIPMCPIVKSIANPEA VQQLIAKLDMNNANPMDCLAYRFDIVLRGQRKTHFENC C:  PIELLPETPSQTAGPYVHIGLALEAAGNPTRDQEIWNRLA KPDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEYQ DAYNLENAFNSFGRTATTFDAGEWTLHTVKPGVVNNAAGV PMAPHINISLFARGINIHLHTRLYFDDEAQANAKCPVLNL IEQPQRRETLIAKRCEVDGKTAYRFDIRIQGEGETVFFDF D:  PAQDNSRFVIRDRNWHPKALTPDYKTSIARSPRQALVSIP QSISETTGPNFSHLGFGAHDHDLLLNFNNGGLPIGERIIV AGRVVDQYGKPVPNTLVEMWQANAGGRCRHKNDRYLAPLD PNFGGVGRXLTDSDGYYSFRTIKPGPYPWRNGPNDWRPAH IHFGISGPSIATKLITQLYFEGDPLIPMCPIVKSIANPEA VQQLIAKLDMNNANPMDCLAYRFDIVLRGQRKTHFENC E:  PIELLPETPSQTAGPYVHIGLALEAAGNPTRDQEIWNRLA KPDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEYQ DAYNLENAFNSFGRTATTFDAGEWTLHTVKPGVVNNAAGV PMAPHINISLFARGINIHLHTRLYFDDEAQANAKCPVLNL IEQPQRRETLIAKRCEVDGKTAYRFDIRIQGEGETVFFDF F:  PAQDNSRFVIRDRNWHPKALTPDYKTSIARSPRQALVSIP QSISETTGPNFSHLGFGAHDHDLLLNFNNGGLPIGERIIV AGRVVDQYGKPVPNTLVEMWQANAGGRCRHKNDRYLAPLD PNFGGVGRXLTDSDGYYSFRTIKPGPYPWRNGPNDWRPAH IHFGISGPSIATKLITQLYFEGDPLIPMCPIVKSIANPEA VQQLIAKLDMNNANPMDCLAYRFDIVLRGQRKTHFENC G:  PIELLPETPSQTAGPYVHIGLALEAAGNPTRDQEIWNRLA KPDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEYQ DAYNLENAFNSFGRTATTFDAGEWTLHTVKPGVVNNAAGV PMAPHINISLFARGINIHLHTRLYFDDEAQANAKCPVLNL IEQPQRRETLIAKRCEVDGKTAYRFDIRIQGEGETVFFDF H:  PAQDNSRFVIRDRNWHPKALTPDYKTSIARSPRQALVSIP QSISETTGPNFSHLGFGAHDHDLLLNFNNGGLPIGERIIV AGRVVDQYGKPVPNTLVEMWQANAGGRCRHKNDRYLAPLD PNFGGVGRXLTDSDGYYSFRTIKPGPYPWRNGPNDWRPAH IHFGISGPSIATKLITQLYFEGDPLIPMCPIVKSIANPEA VQQLIAKLDMNNANPMDCLAYRFDIVLRGQRKTHFENC I:  PIELLPETPSQTAGPYVHIGLALEAAGNPTRDQEIWNRLA KPDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEYQ DAYNLENAFNSFGRTATTFDAGEWTLHTVKPGVVNNAAGV PMAPHINISLFARGINIHLHTRLYFDDEAQANAKCPVLNL IEQPQRRETLIAKRCEVDGKTAYRFDIRIQGEGETVFFDF J:  PAQDNSRFVIRDRNWHPKALTPDYKTSIARSPRQALVSIP QSISETTGPNFSHLGFGAHDHDLLLNFNNGGLPIGERIIV AGRVVDQYGKPVPNTLVEMWQANAGGRCRHKNDRYLAPLD PNFGGVGRXLTDSDGYYSFRTIKPGPYPWRNGPNDWRPAH IHFGISGPSIATKLITQLYFEGDPLIPMCPIVKSIANPEA VQQLIAKLDMNNANPMDCLAYRFDIVLRGQRKTHFENC K:  PIELLPETPSQTAGPYVHIGLALEAAGNPTRDQEIWNRLA KPDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEYQ DAYNLENAFNSFGRTATTFDAGEWTLHTVKPGVVNNAAGV PMAPHINISLFARGINIHLHTRLYFDDEAQANAKCPVLNL IEQPQRRETLIAKRCEVDGKTAYRFDIRIQGEGETVFFDF L:  PAQDNSRFVIRDRNWHPKALTPDYKTSIARSPRQALVSIP QSISETTGPNFSHLGFGAHDHDLLLNFNNGGLPIGERIIV AGRVVDQYGKPVPNTLVEMWQANAGGRCRHKNDRYLAPLD PNFGGVGRXLTDSDGYYSFRTIKPGPYPWRNGPNDWRPAH IHFGISGPSIATKLITQLYFEGDPLIPMCPIVKSIANPEA VQQLIAKLDMNNANPMDCLAYRFDIVLRGQRKTHFENC Description Functional site 1) chain B residue 447 type sequence Y description BINDING SITE FOR RESIDUE FE B 600 source : AC1 2) chain B residue 460 type sequence H description BINDING SITE FOR RESIDUE FE B 600 source : AC1 3) chain B residue 462 type sequence H description BINDING SITE FOR RESIDUE FE B 600 source : AC1 4) chain D residue 447 type sequence Y description BINDING SITE FOR RESIDUE FE D 600 source : AC2 5) chain D residue 460 type sequence H description BINDING SITE FOR RESIDUE FE D 600 source : AC2 6) chain D residue 462 type sequence H description BINDING SITE FOR RESIDUE FE D 600 source : AC2 7) chain F residue 447 type sequence Y description BINDING SITE FOR RESIDUE FE F 600 source : AC3 8) chain F residue 460 type sequence H description BINDING SITE FOR RESIDUE FE F 600 source : AC3 9) chain F residue 462 type sequence H description BINDING SITE FOR RESIDUE FE F 600 source : AC3 10) chain H residue 447 type sequence Y description BINDING SITE FOR RESIDUE FE H 600 source : AC4 11) chain H residue 460 type sequence H description BINDING SITE FOR RESIDUE FE H 600 source : AC4 12) chain H residue 462 type sequence H description BINDING SITE FOR RESIDUE FE H 600 source : AC4 13) chain J residue 447 type sequence Y description BINDING SITE FOR RESIDUE FE J 600 source : AC5 14) chain J residue 460 type sequence H description BINDING SITE FOR RESIDUE FE J 600 source : AC5 15) chain J residue 462 type sequence H description BINDING SITE FOR RESIDUE FE J 600 source : AC5 16) chain L residue 447 type sequence Y description BINDING SITE FOR RESIDUE FE L 600 source : AC6 17) chain L residue 460 type sequence H description BINDING SITE FOR RESIDUE FE L 600 source : AC6 18) chain L residue 462 type sequence H description BINDING SITE FOR RESIDUE FE L 600 source : AC6 19) chain B residue 409 type catalytic sequence R description 936 source MCSA : MCSA1 20) chain B residue 448 type catalytic sequence P description 936 source MCSA : MCSA1 21) chain B residue 458 type catalytic sequence P description 936 source MCSA : MCSA1 22) chain B residue 461 type catalytic sequence I description 936 source MCSA : MCSA1 23) chain B residue 463 type catalytic sequence F description 936 source MCSA : MCSA1 24) chain D residue 409 type catalytic sequence R description 936 source MCSA : MCSA2 25) chain D residue 448 type catalytic sequence P description 936 source MCSA : MCSA2 26) chain D residue 458 type catalytic sequence P description 936 source MCSA : MCSA2 27) chain D residue 461 type catalytic sequence I description 936 source MCSA : MCSA2 28) chain D residue 463 type catalytic sequence F description 936 source MCSA : MCSA2 29) chain F residue 409 type catalytic sequence R description 936 source MCSA : MCSA3 30) chain F residue 448 type catalytic sequence P description 936 source MCSA : MCSA3 31) chain F residue 458 type catalytic sequence P description 936 source MCSA : MCSA3 32) chain F residue 461 type catalytic sequence I description 936 source MCSA : MCSA3 33) chain F residue 463 type catalytic sequence F description 936 source MCSA : MCSA3 34) chain H residue 409 type catalytic sequence R description 936 source MCSA : MCSA4 35) chain H residue 448 type catalytic sequence P description 936 source MCSA : MCSA4 36) chain H residue 458 type catalytic sequence P description 936 source MCSA : MCSA4 37) chain H residue 461 type catalytic sequence I description 936 source MCSA : MCSA4 38) chain H residue 463 type catalytic sequence F description 936 source MCSA : MCSA4 39) chain J residue 409 type catalytic sequence R description 936 source MCSA : MCSA5 40) chain J residue 448 type catalytic sequence P description 936 source MCSA : MCSA5 41) chain J residue 458 type catalytic sequence P description 936 source MCSA : MCSA5 42) chain J residue 461 type catalytic sequence I description 936 source MCSA : MCSA5 43) chain J residue 463 type catalytic sequence F description 936 source MCSA : MCSA5 44) chain L residue 409 type catalytic sequence R description 936 source MCSA : MCSA6 45) chain L residue 448 type catalytic sequence P description 936 source MCSA : MCSA6 46) chain L residue 458 type catalytic sequence P description 936 source MCSA : MCSA6 47) chain L residue 461 type catalytic sequence I description 936 source MCSA : MCSA6 48) chain L residue 463 type catalytic sequence F description 936 source MCSA : MCSA6 49) chain A residue 51-79 type prosite sequence LLGQVYDGNGHLVRDSFLEVWQADANGEY description INTRADIOL_DIOXYGENAS Intradiol ring-cleavage dioxygenases signature. LlGqVydgnGhlVrdsfLEVwqadanGeY source prosite : PS00083 50) chain B residue 409 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 51) chain F residue 448 type BINDING sequence P description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 52) chain F residue 461 type BINDING sequence I description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 53) chain F residue 463 type BINDING sequence F description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 54) chain H residue 409 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 55) chain H residue 448 type BINDING sequence P description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 56) chain H residue 461 type BINDING sequence I description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 57) chain H residue 463 type BINDING sequence F description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 58) chain J residue 409 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 59) chain J residue 448 type BINDING sequence P description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 60) chain J residue 461 type BINDING sequence I description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 61) chain B residue 448 type BINDING sequence P description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 62) chain J residue 463 type BINDING sequence F description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 63) chain L residue 409 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 64) chain L residue 448 type BINDING sequence P description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 65) chain L residue 461 type BINDING sequence I description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 66) chain L residue 463 type BINDING sequence F description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 67) chain B residue 461 type BINDING sequence I description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 68) chain B residue 463 type BINDING sequence F description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 69) chain D residue 409 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 70) chain D residue 448 type BINDING sequence P description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 71) chain D residue 461 type BINDING sequence I description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 72) chain D residue 463 type BINDING sequence F description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 73) chain F residue 409 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1

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