eF-site ID 1ax4-ABCD PDB Code 1ax4 Chain A, B, C, D click to enlarge Title TRYPTOPHANASE FROM PROTEUS VULGARIS Classification TRYPTOPHAN BIOSYNTHESIS Compound TRYPTOPHANASE Source (TNAA_PROVU) Sequence A:  AKRIVEPFRIKMVEKIRVPSREEREAALKEAGYNPFLLPS SAVYIDLLTDSGTNAMSDHQWAAMITGDEAYAGSRNYYDL KDKAKELFNYDYIIPAHQGRGAENILFPVLLKYKQKEGKA KNPVFISNFHFDTTAAHVELNGCKAINIVTEKAFDSETYD DWKGDFDIKKLKENIAQHGADNIVAIVSTVTCNSAGGQPV SMSNLKEVYEIAKQHGIFVVMDSARFCENAYFIKARDPKY KNATIKEVIFDMYKYADALTMSAKXDPLLNIGGLVAIRDN EEIFTLARQRCVPMEGFVTYGGLAGRDMAAMVQGLEEGTE EEYLHYRIGQVKYLGDRLREAGIPIQYPTGGHAVFVDCKK LVPQIPGDQFPAQAVINALYLESGVRAVEIGSFLLGRDPA TGEQKHADMEFMRLTIARRVYTNDHMDYIADALIGLKEKF ATLKGLEFEYEPPVLRHFTARLKPI B:  AKRIVEPFRIKMVEKIRVPSREEREAALKEAGYNPFLLPS SAVYIDLLTDSGTNAMSDHQWAAMITGDEAYAGSRNYYDL KDKAKELFNYDYIIPAHQGRGAENILFPVLLKYKQKEGKA KNPVFISNFHFDTTAAHVELNGCKAINIVTEKAFDSETYD DWKGDFDIKKLKENIAQHGADNIVAIVSTVTCNSAGGQPV SMSNLKEVYEIAKQHGIFVVMDSARFCENAYFIKARDPKY KNATIKEVIFDMYKYADALTMSAKXDPLLNIGGLVAIRDN EEIFTLARQRCVPMEGFVTYGGLAGRDMAAMVQGLEEGTE EEYLHYRIGQVKYLGDRLREAGIPIQYPTGGHAVFVDCKK LVPQIPGDQFPAQAVINALYLESGVRAVEIGSFLLGRDPA TGEQKHADMEFMRLTIARRVYTNDHMDYIADALIGLKEKF ATLKGLEFEYEPPVLRHFTARLKPI C:  AKRIVEPFRIKMVEKIRVPSREEREAALKEAGYNPFLLPS SAVYIDLLTDSGTNAMSDHQWAAMITGDEAYAGSRNYYDL KDKAKELFNYDYIIPAHQGRGAENILFPVLLKYKQKEGKA KNPVFISNFHFDTTAAHVELNGCKAINIVTEKAFDSETYD DWKGDFDIKKLKENIAQHGADNIVAIVSTVTCNSAGGQPV SMSNLKEVYEIAKQHGIFVVMDSARFCENAYFIKARDPKY KNATIKEVIFDMYKYADALTMSAKXDPLLNIGGLVAIRDN EEIFTLARQRCVPMEGFVTYGGLAGRDMAAMVQGLEEGTE EEYLHYRIGQVKYLGDRLREAGIPIQYPTGGHAVFVDCKK LVPQIPGDQFPAQAVINALYLESGVRAVEIGSFLLGRDPA TGEQKHADMEFMRLTIARRVYTNDHMDYIADALIGLKEKF ATLKGLEFEYEPPVLRHFTARLKPI D:  AKRIVEPFRIKMVEKIRVPSREEREAALKEAGYNPFLLPS SAVYIDLLTDSGTNAMSDHQWAAMITGDEAYAGSRNYYDL KDKAKELFNYDYIIPAHQGRGAENILFPVLLKYKQKEGKA KNPVFISNFHFDTTAAHVELNGCKAINIVTEKAFDSETYD DWKGDFDIKKLKENIAQHGADNIVAIVSTVTCNSAGGQPV SMSNLKEVYEIAKQHGIFVVMDSARFCENAYFIKARDPKY KNATIKEVIFDMYKYADALTMSAKXDPLLNIGGLVAIRDN EEIFTLARQRCVPMEGFVTYGGLAGRDMAAMVQGLEEGTE EEYLHYRIGQVKYLGDRLREAGIPIQYPTGGHAVFVDCKK LVPQIPGDQFPAQAVINALYLESGVRAVEIGSFLLGRDPA TGEQKHADMEFMRLTIARRVYTNDHMDYIADALIGLKEKF ATLKGLEFEYEPPVLRHFTARLKPI Description Functional site 1) chain A residue 70 type sequence E description POTASSIUM BINDING SITE. source : POA 2) chain B residue 53 type sequence G description POTASSIUM BINDING SITE. source : POA 3) chain B residue 271 type sequence N description POTASSIUM BINDING SITE. source : POA 4) chain B residue 70 type sequence E description POTASSIUM BINDING SITE. source : POB 5) chain A residue 53 type sequence G description POTASSIUM BINDING SITE. source : POB 6) chain A residue 271 type sequence N description POTASSIUM BINDING SITE. source : POB 7) chain C residue 70 type sequence E description POTASSIUM BINDING SITE. source : POC 8) chain D residue 53 type sequence G description POTASSIUM BINDING SITE. source : POC 9) chain D residue 271 type sequence N description POTASSIUM BINDING SITE. source : POC 10) chain D residue 70 type sequence E description POTASSIUM BINDING SITE. source : POD 11) chain C residue 53 type sequence G description POTASSIUM BINDING SITE. source : POD 12) chain C residue 271 type sequence N description POTASSIUM BINDING SITE. source : POD 13) chain A residue 266 type sequence X description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPA 14) chain A residue 226 type sequence R description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPA 15) chain A residue 222 type sequence M description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPA 16) chain A residue 194 type sequence N description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPA 17) chain A residue 132 type sequence F description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPA 18) chain A residue 225 type sequence A description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPA 19) chain A residue 100 type sequence G description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPA 20) chain A residue 101 type sequence R description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPA 21) chain A residue 99 type sequence Q description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPA 22) chain A residue 263 type sequence S description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPA 23) chain A residue 52 type sequence S description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPA 24) chain A residue 265 type sequence K description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPA 25) chain B residue 72 type sequence Y description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPA 26) chain B residue 301 type sequence Y description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPA 27) chain B residue 266 type sequence X description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPB 28) chain B residue 226 type sequence R description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPB 29) chain B residue 222 type sequence M description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPB 30) chain B residue 194 type sequence N description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPB 31) chain B residue 132 type sequence F description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPB 32) chain B residue 225 type sequence A description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPB 33) chain B residue 100 type sequence G description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPB 34) chain B residue 101 type sequence R description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPB 35) chain B residue 99 type sequence Q description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPB 36) chain B residue 263 type sequence S description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPB 37) chain B residue 52 type sequence S description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPB 38) chain B residue 265 type sequence K description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPB 39) chain A residue 72 type sequence Y description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPB 40) chain A residue 301 type sequence Y description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPB 41) chain C residue 266 type sequence X description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPC 42) chain C residue 226 type sequence R description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPC 43) chain C residue 222 type sequence M description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPC 44) chain C residue 194 type sequence N description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPC 45) chain C residue 132 type sequence F description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPC 46) chain C residue 225 type sequence A description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPC 47) chain C residue 100 type sequence G description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPC 48) chain C residue 101 type sequence R description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPC 49) chain C residue 99 type sequence Q description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPC 50) chain C residue 263 type sequence S description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPC 51) chain C residue 52 type sequence S description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPC 52) chain C residue 265 type sequence K description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPC 53) chain D residue 72 type sequence Y description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPC 54) chain D residue 301 type sequence Y description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPC 55) chain D residue 266 type sequence X description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPD 56) chain D residue 226 type sequence R description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPD 57) chain D residue 222 type sequence M description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPD 58) chain D residue 194 type sequence N description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPD 59) chain D residue 132 type sequence F description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPD 60) chain D residue 225 type sequence A description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPD 61) chain D residue 100 type sequence G description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPD 62) chain D residue 101 type sequence R description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPD 63) chain D residue 99 type sequence Q description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPD 64) chain D residue 263 type sequence S description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPD 65) chain D residue 52 type sequence S description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPD 66) chain D residue 265 type sequence K description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPD 67) chain C residue 72 type sequence Y description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPD 68) chain C residue 301 type sequence Y description PYRIDOXAL 5'-PHOSPHATE BINDING SITE. source : LPD 69) chain A residue 53 type sequence G description BINDING SITE FOR RESIDUE K A 500 source : AC1 70) chain A residue 271 type sequence N description BINDING SITE FOR RESIDUE K A 500 source : AC1 71) chain B residue 70 type sequence E description BINDING SITE FOR RESIDUE K A 500 source : AC1 72) chain A residue 70 type sequence E description BINDING SITE FOR RESIDUE K B 500 source : AC2 73) chain B residue 53 type sequence G description BINDING SITE FOR RESIDUE K B 500 source : AC2 74) chain B residue 271 type sequence N description BINDING SITE FOR RESIDUE K B 500 source : AC2 75) chain C residue 53 type sequence G description BINDING SITE FOR RESIDUE K C 500 source : AC3 76) chain C residue 271 type sequence N description BINDING SITE FOR RESIDUE K C 500 source : AC3 77) chain D residue 70 type sequence E description BINDING SITE FOR RESIDUE K C 500 source : AC3 78) chain C residue 70 type sequence E description BINDING SITE FOR RESIDUE K D 500 source : AC4 79) chain D residue 53 type sequence G description BINDING SITE FOR RESIDUE K D 500 source : AC4 80) chain D residue 271 type sequence N description BINDING SITE FOR RESIDUE K D 500 source : AC4 81) chain A residue 72 type catalytic sequence Y description 410 source MCSA : MCSA1 82) chain A residue 132 type catalytic sequence F description 410 source MCSA : MCSA1 83) chain A residue 133 type catalytic sequence D description 410 source MCSA : MCSA1 84) chain A residue 223 type catalytic sequence D description 410 source MCSA : MCSA1 85) chain A residue 225 type catalytic sequence A description 410 source MCSA : MCSA1 86) chain A residue 266 type catalytic sequence X description 410 source MCSA : MCSA1 87) chain A residue 458 type catalytic sequence H description 410 source MCSA : MCSA1 88) chain B residue 72 type catalytic sequence Y description 410 source MCSA : MCSA2 89) chain B residue 132 type catalytic sequence F description 410 source MCSA : MCSA2 90) chain B residue 133 type catalytic sequence D description 410 source MCSA : MCSA2 91) chain B residue 223 type catalytic sequence D description 410 source MCSA : MCSA2 92) chain B residue 225 type catalytic sequence A description 410 source MCSA : MCSA2 93) chain B residue 266 type catalytic sequence X description 410 source MCSA : MCSA2 94) chain B residue 458 type catalytic sequence H description 410 source MCSA : MCSA2 95) chain C residue 72 type catalytic sequence Y description 410 source MCSA : MCSA3 96) chain C residue 132 type catalytic sequence F description 410 source MCSA : MCSA3 97) chain C residue 133 type catalytic sequence D description 410 source MCSA : MCSA3 98) chain C residue 223 type catalytic sequence D description 410 source MCSA : MCSA3 99) chain C residue 225 type catalytic sequence A description 410 source MCSA : MCSA3 100) chain C residue 266 type catalytic sequence X description 410 source MCSA : MCSA3 101) chain C residue 458 type catalytic sequence H description 410 source MCSA : MCSA3 102) chain D residue 72 type catalytic sequence Y description 410 source MCSA : MCSA4 103) chain D residue 132 type catalytic sequence F description 410 source MCSA : MCSA4 104) chain D residue 133 type catalytic sequence D description 410 source MCSA : MCSA4 105) chain D residue 223 type catalytic sequence D description 410 source MCSA : MCSA4 106) chain D residue 225 type catalytic sequence A description 410 source MCSA : MCSA4 107) chain D residue 266 type catalytic sequence X description 410 source MCSA : MCSA4 108) chain D residue 458 type catalytic sequence H description 410 source MCSA : MCSA4 109) chain A residue 256-274 type prosite sequence YADALTMSAKXDPLLNIGG description BETA_ELIM_LYASE Beta-eliminating lyases pyridoxal-phosphate attachment site. YaDaltMSAKKDpLLnIGG source prosite : PS00853 110) chain A residue 266 type MOD_RES sequence X description N6-(pyridoxal phosphate)lysine source Swiss-Prot : SWS_FT_FI1 111) chain B residue 266 type MOD_RES sequence X description N6-(pyridoxal phosphate)lysine source Swiss-Prot : SWS_FT_FI1 112) chain C residue 266 type MOD_RES sequence X description N6-(pyridoxal phosphate)lysine source Swiss-Prot : SWS_FT_FI1 113) chain D residue 266 type MOD_RES sequence X description N6-(pyridoxal phosphate)lysine source Swiss-Prot : SWS_FT_FI1

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