eF-site ID 3pcn-N PDB Code 3pcn Chain N click to enlarge Title STRUCTURE OF PROTOCATECHUATE 3,4-DIOXYGENASE COMPLEXED WITH 3,4-DIHYDROXYPHENYLACETATE Classification DIOXYGENASE Compound PROTOCATECHUATE 3,4-DIOXYGENASE Source ORGANISM_SCIENTIFIC: Pseudomonas putida; Sequence N:  PAQDNSRFVIRDRNWHPKALTPDYKTSIARSPRQALVSIP QSISETTGPNFSHLGFGAHDHDLLLNFGLPIGERIIVAGR VVDQYGKPVPNTLVEMWQANAGGRYRHKNDRYLAPLDPNF GGVGRCLTDSDGYYSFRTIKPGPYPWRNGPNDWRPAHIHF GISGPSIATKLITQLYFEGDPLIPMCPIVKSIANPEAVQQ LIAKLDMNNANPMDCLAYRFDIVLRGQRKTHFE Description Functional site 1) chain N residue 324 type sequence Y description SITE "ACB" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : ACB 2) chain N residue 326 type sequence T description SITE "ACB" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : ACB 3) chain N residue 400 type sequence W description SITE "ACB" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : ACB 4) chain N residue 408 type sequence Y description SITE "ACB" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : ACB 5) chain N residue 413 type sequence D description SITE "ACB" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : ACB 6) chain N residue 447 type sequence Y description SITE "ACB" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : ACB 7) chain N residue 448 type sequence P description SITE "ACB" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : ACB 8) chain N residue 449 type sequence W description SITE "ACB" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : ACB 9) chain N residue 450 type sequence R description SITE "ACB" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : ACB 10) chain N residue 457 type sequence R description SITE "ACB" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : ACB 11) chain N residue 460 type sequence H description SITE "ACB" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : ACB 12) chain N residue 462 type sequence H description SITE "ACB" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : ACB 13) chain N residue 477 type sequence Q description SITE "ACB" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : ACB 14) chain N residue 491 type sequence I description SITE "ACB" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : ACB 15) chain N residue 304 type sequence D description SITE "VEB" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : VEB 16) chain N residue 307 type sequence R description SITE "VEB" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : VEB 17) chain N residue 339 type sequence I description SITE "VEB" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : VEB 18) chain N residue 340 type sequence P description SITE "VEB" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : VEB 19) chain N residue 341 type sequence Q description SITE "VEB" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : VEB 20) chain N residue 342 type sequence S description SITE "VEB" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : VEB 21) chain N residue 343 type sequence I description SITE "VEB" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : VEB 22) chain N residue 344 type sequence S description SITE "VEB" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : VEB 23) chain N residue 345 type sequence E description SITE "VEB" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. source : VEB 24) chain N residue 408 type sequence Y description BINDING SITE FOR RESIDUE FE N 600 source : AC2 25) chain N residue 460 type sequence H description BINDING SITE FOR RESIDUE FE N 600 source : AC2 26) chain N residue 462 type sequence H description BINDING SITE FOR RESIDUE FE N 600 source : AC2 27) chain N residue 361 type sequence H description BINDING SITE FOR RESIDUE BME N 601 source : AC9 28) chain N residue 429 type sequence C description BINDING SITE FOR RESIDUE BME N 601 source : AC9 29) chain N residue 438 type sequence S description BINDING SITE FOR RESIDUE BME N 601 source : AC9 30) chain N residue 324 type sequence Y description BINDING SITE FOR RESIDUE DHY N 550 source : BC1 31) chain N residue 408 type sequence Y description BINDING SITE FOR RESIDUE DHY N 550 source : BC1 32) chain N residue 447 type sequence Y description BINDING SITE FOR RESIDUE DHY N 550 source : BC1 33) chain N residue 449 type sequence W description BINDING SITE FOR RESIDUE DHY N 550 source : BC1 34) chain N residue 457 type sequence R description BINDING SITE FOR RESIDUE DHY N 550 source : BC1 35) chain N residue 460 type sequence H description BINDING SITE FOR RESIDUE DHY N 550 source : BC1 36) chain N residue 462 type sequence H description BINDING SITE FOR RESIDUE DHY N 550 source : BC1 37) chain N residue 491 type sequence I description BINDING SITE FOR RESIDUE DHY N 550 source : BC1 38) chain N residue 409 type catalytic sequence R description 936 source MCSA : MCSA2 39) chain N residue 448 type catalytic sequence P description 936 source MCSA : MCSA2 40) chain N residue 458 type catalytic sequence P description 936 source MCSA : MCSA2 41) chain N residue 461 type catalytic sequence I description 936 source MCSA : MCSA2 42) chain N residue 463 type catalytic sequence F description 936 source MCSA : MCSA2 43) chain N residue 409 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 44) chain N residue 448 type BINDING sequence P description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 45) chain N residue 461 type BINDING sequence I description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1 46) chain N residue 463 type BINDING sequence F description BINDING => ECO:0000269|PubMed:7990141 source Swiss-Prot : SWS_FT_FI1

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