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 null (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 BINDING sequence R description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 448 type BINDING sequence P description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 461 type BINDING sequence I description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 22) chain B residue 463 type BINDING sequence F description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 23) chain D residue 409 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 24) chain D residue 448 type BINDING sequence P description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 25) chain D residue 461 type BINDING sequence I description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 26) chain D residue 463 type BINDING sequence F description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 27) chain F residue 409 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 28) chain F residue 448 type BINDING sequence P description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 29) chain F residue 461 type BINDING sequence I description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 30) chain F residue 463 type BINDING sequence F description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 31) chain H residue 409 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 32) chain H residue 448 type BINDING sequence P description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 33) chain H residue 461 type BINDING sequence I description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 34) chain H residue 463 type BINDING sequence F description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 35) chain J residue 409 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 36) chain J residue 448 type BINDING sequence P description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 37) chain J residue 461 type BINDING sequence I description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 38) chain J residue 463 type BINDING sequence F description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 39) chain L residue 409 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 40) chain L residue 448 type BINDING sequence P description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 41) chain L residue 461 type BINDING sequence I description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 42) chain L residue 463 type BINDING sequence F description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 51-79 type prosite sequence LLGQVYDGNGHLVRDSFLEVWQADANGEY description INTRADIOL_DIOXYGENAS Intradiol ring-cleavage dioxygenases signature. LlGqVydgnGhlVrdsfLEVwqadanGeY source prosite : PS00083 44) chain B residue 409 type catalytic sequence R description 936 source MCSA : MCSA1 45) chain B residue 448 type catalytic sequence P description 936 source MCSA : MCSA1 46) chain B residue 458 type catalytic sequence P description 936 source MCSA : MCSA1 47) chain B residue 461 type catalytic sequence I description 936 source MCSA : MCSA1 48) chain B residue 463 type catalytic sequence F description 936 source MCSA : MCSA1 49) chain D residue 409 type catalytic sequence R description 936 source MCSA : MCSA2 50) chain D residue 448 type catalytic sequence P description 936 source MCSA : MCSA2 51) chain D residue 458 type catalytic sequence P description 936 source MCSA : MCSA2 52) chain D residue 461 type catalytic sequence I description 936 source MCSA : MCSA2 53) chain D residue 463 type catalytic sequence F description 936 source MCSA : MCSA2 54) chain F residue 409 type catalytic sequence R description 936 source MCSA : MCSA3 55) chain F residue 448 type catalytic sequence P description 936 source MCSA : MCSA3 56) chain F residue 458 type catalytic sequence P description 936 source MCSA : MCSA3 57) chain F residue 461 type catalytic sequence I description 936 source MCSA : MCSA3 58) chain F residue 463 type catalytic sequence F description 936 source MCSA : MCSA3 59) chain H residue 409 type catalytic sequence R description 936 source MCSA : MCSA4 60) chain H residue 448 type catalytic sequence P description 936 source MCSA : MCSA4 61) chain H residue 458 type catalytic sequence P description 936 source MCSA : MCSA4 62) chain H residue 461 type catalytic sequence I description 936 source MCSA : MCSA4 63) chain H residue 463 type catalytic sequence F description 936 source MCSA : MCSA4 64) chain J residue 409 type catalytic sequence R description 936 source MCSA : MCSA5 65) chain J residue 448 type catalytic sequence P description 936 source MCSA : MCSA5 66) chain J residue 458 type catalytic sequence P description 936 source MCSA : MCSA5 67) chain J residue 461 type catalytic sequence I description 936 source MCSA : MCSA5 68) chain J residue 463 type catalytic sequence F description 936 source MCSA : MCSA5 69) chain L residue 409 type catalytic sequence R description 936 source MCSA : MCSA6 70) chain L residue 448 type catalytic sequence P description 936 source MCSA : MCSA6 71) chain L residue 458 type catalytic sequence P description 936 source MCSA : MCSA6 72) chain L residue 461 type catalytic sequence I description 936 source MCSA : MCSA6 73) chain L residue 463 type catalytic sequence F description 936 source MCSA : MCSA6

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