eF-site ID 3fsl-ABCDEF PDB Code 3fsl Chain A, B, C, D, E, F click to enlarge Title Crystal structure of tyrosine aminotransferase tripple mutant (P181Q,R183G,A321K) from Escherichia coli at 2.35 A resolution Classification TRANSFERASE Compound Aromatic-amino-acid aminotransferase Source null (TYRB_ECOLI) Sequence A:  MFQKVDAYAGDPILTLMERFKEDPRSDKVNLSIGLYYNED GIIPQLQAVAEAEARLNAQPHGASLYLPMEGLNCYRHAIA PLLFGADHPVLKQQRVATIQTLGGSGALKVGADFLKRYFP ESGVWVSDPTWENHVAIFAGAGFEVSTYPWYDEATNGVRF NDLLATLKTLQAGSIVLLHPCCHNPTGADLTNDQWDAVIE ILKARELIPFLDIAYQGFGAGMEEDAYAIRAIASAGLPAL VSNSFSKIFSLYGERVGGLSVMCEDAEAAGRVLGQLKATV RRNYSSPPNFGAQVVAAVLNDEALKASWLKEVEEMRTRIL AMRQELVKVLSTEMPERNFDYLLNQRGMFSYTGLSAAQVD RLREEFGVYLIASGRMCVAGLNTANVQRVAKAFAAVM B:  MFQKVDAYAGDPILTLMERFKEDPRSDKVNLSIGLYYNED GIIPQLQAVAEAEARLNAQPHGASLYLPMEGLNCYRHAIA PLLFGADHPVLKQQRVATIQTLGGSGALKVGADFLKRYFP ESGVWVSDPTWENHVAIFAGAGFEVSTYPWYDEATNGVRF NDLLATLKTLQAGSIVLLHPCCHNPTGADLTNDQWDAVIE ILKARELIPFLDIAYQGFGAGMEEDAYAIRAIASAGLPAL VSNSFSKIFSLYGERVGGLSVMCEDAEAAGRVLGQLKATV RRNYSSPPNFGAQVVAAVLNDEALKASWLKEVEEMRTRIL AMRQELVKVLSTEMPERNFDYLLNQRGMFSYTGLSAAQVD RLREEFGVYLIASGRMCVAGLNTANVQRVAKAFAAVM C:  MFQKVDAYAGDPILTLMERFKEDPRSDKVNLSIGLYYNED GIIPQLQAVAEAEARLNAQPHGASLYLPMEGLNCYRHAIA PLLFGADHPVLKQQRVATIQTLGGSGALKVGADFLKRYFP ESGVWVSDPTWENHVAIFAGAGFEVSTYPWYDEATNGVRF NDLLATLKTLQAGSIVLLHPCCHNPTGADLTNDQWDAVIE ILKARELIPFLDIAYQGFGAGMEEDAYAIRAIASAGLPAL VSNSFSKIFSLYGERVGGLSVMCEDAEAAGRVLGQLKATV RRNYSSPPNFGAQVVAAVLNDEALKASWLKEVEEMRTRIL AMRQELVKVLSTEMPERNFDYLLNQRGMFSYTGLSAAQVD RLREEFGVYLIASGRMCVAGLNTANVQRVAKAFAAVM D:  MFQKVDAYAGDPILTLMERFKEDPRSDKVNLSIGLYYNED GIIPQLQAVAEAEARLNAQPHGASLYLPMEGLNCYRHAIA PLLFGADHPVLKQQRVATIQTLGGSGALKVGADFLKRYFP ESGVWVSDPTWENHVAIFAGAGFEVSTYPWYDEATNGVRF NDLLATLKTLQAGSIVLLHPCCHNPTGADLTNDQWDAVIE ILKARELIPFLDIAYQGFGAGMEEDAYAIRAIASAGLPAL VSNSFSKIFSLYGERVGGLSVMCEDAEAAGRVLGQLKATV RRNYSSPPNFGAQVVAAVLNDEALKASWLKEVEEMRTRIL AMRQELVKVLSTEMPERNFDYLLNQRGMFSYTGLSAAQVD RLREEFGVYLIASGRMCVAGLNTANVQRVAKAFAAVM E:  MFQKVDAYAGDPILTLMERFKEDPRSDKVNLSIGLYYNED GIIPQLQAVAEAEARLNAQPHGASLYLPMEGLNCYRHAIA PLLFGADHPVLKQQRVATIQTLGGSGALKVGADFLKRYFP ESGVWVSDPTWENHVAIFAGAGFEVSTYPWYDEATNGVRF NDLLATLKTLQAGSIVLLHPCCHNPTGADLTNDQWDAVIE ILKARELIPFLDIAYQGFGAGMEEDAYAIRAIASAGLPAL VSNSFSKIFSLYGERVGGLSVMCEDAEAAGRVLGQLKATV RRNYSSPPNFGAQVVAAVLNDEALKASWLKEVEEMRTRIL AMRQELVKVLSTEMPERNFDYLLNQRGMFSYTGLSAAQVD RLREEFGVYLIASGRMCVAGLNTANVQRVAKAFAAVM F:  MFQKVDAYAGDPILTLMERFKEDPRSDKVNLSIGLYYNED GIIPQLQAVAEAEARLNAQPHGASLYLPMEGLNCYRHAIA PLLFGADHPVLKQQRVATIQTLGGSGALKVGADFLKRYFP ESGVWVSDPTWENHVAIFAGAGFEVSTYPWYDEATNGVRF NDLLATLKTLQAGSIVLLHPCCHNPTGADLTNDQWDAVIE ILKARELIPFLDIAYQGFGAGMEEDAYAIRAIASAGLPAL VSNSFSKIFSLYGERVGGLSVMCEDAEAAGRVLGQLKATV RRNYSSPPNFGAQVVAAVLNDEALKASWLKEVEEMRTRIL AMRQELVKVLSTEMPERNFDYLLNQRGMFSYTGLSAAQVD RLREEFGVYLIASGRMCVAGLNTANVQRVAKAFAAVM Description Functional site 1) chain A residue 107 type sequence G description BINDING SITE FOR RESIDUE PLR A 500 source : AC1 2) chain A residue 108 type sequence G description BINDING SITE FOR RESIDUE PLR A 500 source : AC1 3) chain A residue 109 type sequence S description BINDING SITE FOR RESIDUE PLR A 500 source : AC1 4) chain A residue 140 type sequence W description BINDING SITE FOR RESIDUE PLR A 500 source : AC1 5) chain A residue 194 type sequence N description BINDING SITE FOR RESIDUE PLR A 500 source : AC1 6) chain A residue 222 type sequence D description BINDING SITE FOR RESIDUE PLR A 500 source : AC1 7) chain A residue 224 type sequence A description BINDING SITE FOR RESIDUE PLR A 500 source : AC1 8) chain A residue 225 type sequence Y description BINDING SITE FOR RESIDUE PLR A 500 source : AC1 9) chain A residue 255 type sequence S description BINDING SITE FOR RESIDUE PLR A 500 source : AC1 10) chain A residue 257 type sequence S description BINDING SITE FOR RESIDUE PLR A 500 source : AC1 11) chain A residue 258 type sequence K description BINDING SITE FOR RESIDUE PLR A 500 source : AC1 12) chain A residue 266 type sequence R description BINDING SITE FOR RESIDUE PLR A 500 source : AC1 13) chain B residue 70 type sequence Y description BINDING SITE FOR RESIDUE PLR A 500 source : AC1 14) chain A residue 70 type sequence Y description BINDING SITE FOR RESIDUE PLR B 500 source : AC2 15) chain B residue 107 type sequence G description BINDING SITE FOR RESIDUE PLR B 500 source : AC2 16) chain B residue 108 type sequence G description BINDING SITE FOR RESIDUE PLR B 500 source : AC2 17) chain B residue 109 type sequence S description BINDING SITE FOR RESIDUE PLR B 500 source : AC2 18) chain B residue 140 type sequence W description BINDING SITE FOR RESIDUE PLR B 500 source : AC2 19) chain B residue 194 type sequence N description BINDING SITE FOR RESIDUE PLR B 500 source : AC2 20) chain B residue 222 type sequence D description BINDING SITE FOR RESIDUE PLR B 500 source : AC2 21) chain B residue 224 type sequence A description BINDING SITE FOR RESIDUE PLR B 500 source : AC2 22) chain B residue 225 type sequence Y description BINDING SITE FOR RESIDUE PLR B 500 source : AC2 23) chain B residue 255 type sequence S description BINDING SITE FOR RESIDUE PLR B 500 source : AC2 24) chain B residue 257 type sequence S description BINDING SITE FOR RESIDUE PLR B 500 source : AC2 25) chain B residue 258 type sequence K description BINDING SITE FOR RESIDUE PLR B 500 source : AC2 26) chain B residue 266 type sequence R description BINDING SITE FOR RESIDUE PLR B 500 source : AC2 27) chain C residue 107 type sequence G description BINDING SITE FOR RESIDUE PLR C 500 source : AC3 28) chain C residue 108 type sequence G description BINDING SITE FOR RESIDUE PLR C 500 source : AC3 29) chain C residue 109 type sequence S description BINDING SITE FOR RESIDUE PLR C 500 source : AC3 30) chain C residue 140 type sequence W description BINDING SITE FOR RESIDUE PLR C 500 source : AC3 31) chain C residue 194 type sequence N description BINDING SITE FOR RESIDUE PLR C 500 source : AC3 32) chain C residue 222 type sequence D description BINDING SITE FOR RESIDUE PLR C 500 source : AC3 33) chain C residue 224 type sequence A description BINDING SITE FOR RESIDUE PLR C 500 source : AC3 34) chain C residue 225 type sequence Y description BINDING SITE FOR RESIDUE PLR C 500 source : AC3 35) chain C residue 255 type sequence S description BINDING SITE FOR RESIDUE PLR C 500 source : AC3 36) chain C residue 257 type sequence S description BINDING SITE FOR RESIDUE PLR C 500 source : AC3 37) chain C residue 258 type sequence K description BINDING SITE FOR RESIDUE PLR C 500 source : AC3 38) chain C residue 266 type sequence R description BINDING SITE FOR RESIDUE PLR C 500 source : AC3 39) chain D residue 70 type sequence Y description BINDING SITE FOR RESIDUE PLR C 500 source : AC3 40) chain C residue 70 type sequence Y description BINDING SITE FOR RESIDUE PLR D 500 source : AC4 41) chain D residue 107 type sequence G description BINDING SITE FOR RESIDUE PLR D 500 source : AC4 42) chain D residue 108 type sequence G description BINDING SITE FOR RESIDUE PLR D 500 source : AC4 43) chain D residue 109 type sequence S description BINDING SITE FOR RESIDUE PLR D 500 source : AC4 44) chain D residue 140 type sequence W description BINDING SITE FOR RESIDUE PLR D 500 source : AC4 45) chain D residue 194 type sequence N description BINDING SITE FOR RESIDUE PLR D 500 source : AC4 46) chain D residue 222 type sequence D description BINDING SITE FOR RESIDUE PLR D 500 source : AC4 47) chain D residue 224 type sequence A description BINDING SITE FOR RESIDUE PLR D 500 source : AC4 48) chain D residue 225 type sequence Y description BINDING SITE FOR RESIDUE PLR D 500 source : AC4 49) chain D residue 255 type sequence S description BINDING SITE FOR RESIDUE PLR D 500 source : AC4 50) chain D residue 257 type sequence S description BINDING SITE FOR RESIDUE PLR D 500 source : AC4 51) chain D residue 258 type sequence K description BINDING SITE FOR RESIDUE PLR D 500 source : AC4 52) chain D residue 266 type sequence R description BINDING SITE FOR RESIDUE PLR D 500 source : AC4 53) chain E residue 107 type sequence G description BINDING SITE FOR RESIDUE PLR E 500 source : AC5 54) chain E residue 108 type sequence G description BINDING SITE FOR RESIDUE PLR E 500 source : AC5 55) chain E residue 109 type sequence S description BINDING SITE FOR RESIDUE PLR E 500 source : AC5 56) chain E residue 140 type sequence W description BINDING SITE FOR RESIDUE PLR E 500 source : AC5 57) chain E residue 194 type sequence N description BINDING SITE FOR RESIDUE PLR E 500 source : AC5 58) chain E residue 222 type sequence D description BINDING SITE FOR RESIDUE PLR E 500 source : AC5 59) chain E residue 224 type sequence A description BINDING SITE FOR RESIDUE PLR E 500 source : AC5 60) chain E residue 225 type sequence Y description BINDING SITE FOR RESIDUE PLR E 500 source : AC5 61) chain E residue 255 type sequence S description BINDING SITE FOR RESIDUE PLR E 500 source : AC5 62) chain E residue 257 type sequence S description BINDING SITE FOR RESIDUE PLR E 500 source : AC5 63) chain E residue 258 type sequence K description BINDING SITE FOR RESIDUE PLR E 500 source : AC5 64) chain E residue 266 type sequence R description BINDING SITE FOR RESIDUE PLR E 500 source : AC5 65) chain F residue 70 type sequence Y description BINDING SITE FOR RESIDUE PLR E 500 source : AC5 66) chain E residue 70 type sequence Y description BINDING SITE FOR RESIDUE PLR F 500 source : AC6 67) chain F residue 107 type sequence G description BINDING SITE FOR RESIDUE PLR F 500 source : AC6 68) chain F residue 108 type sequence G description BINDING SITE FOR RESIDUE PLR F 500 source : AC6 69) chain F residue 109 type sequence S description BINDING SITE FOR RESIDUE PLR F 500 source : AC6 70) chain F residue 140 type sequence W description BINDING SITE FOR RESIDUE PLR F 500 source : AC6 71) chain F residue 194 type sequence N description BINDING SITE FOR RESIDUE PLR F 500 source : AC6 72) chain F residue 222 type sequence D description BINDING SITE FOR RESIDUE PLR F 500 source : AC6 73) chain F residue 224 type sequence A description BINDING SITE FOR RESIDUE PLR F 500 source : AC6 74) chain F residue 225 type sequence Y description BINDING SITE FOR RESIDUE PLR F 500 source : AC6 75) chain F residue 255 type sequence S description BINDING SITE FOR RESIDUE PLR F 500 source : AC6 76) chain F residue 257 type sequence S description BINDING SITE FOR RESIDUE PLR F 500 source : AC6 77) chain F residue 258 type sequence K description BINDING SITE FOR RESIDUE PLR F 500 source : AC6 78) chain F residue 266 type sequence R description BINDING SITE FOR RESIDUE PLR F 500 source : AC6 79) chain B residue 194 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 80) chain B residue 292 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 81) chain B residue 386 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 82) chain C residue 38 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 83) chain C residue 70 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 84) chain C residue 140 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 85) chain C residue 194 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 86) chain C residue 292 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 87) chain C residue 386 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 88) chain D residue 38 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 89) chain D residue 70 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 90) chain D residue 140 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 91) chain D residue 194 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 92) chain D residue 292 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 93) chain D residue 386 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 94) chain E residue 38 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 95) chain E residue 70 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 96) chain E residue 140 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 97) chain E residue 194 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 98) chain E residue 292 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 99) chain E residue 386 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 100) chain F residue 38 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 101) chain F residue 70 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 102) chain F residue 140 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 103) chain F residue 194 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 104) chain F residue 292 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 105) chain F residue 386 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 106) chain B residue 38 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 107) chain B residue 70 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 108) chain B residue 140 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 109) chain A residue 140 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 110) chain A residue 194 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 111) chain A residue 292 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 112) chain A residue 386 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 113) chain A residue 38 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 114) chain A residue 70 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 115) chain C residue 258 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine source Swiss-Prot : SWS_FT_FI2 116) chain D residue 258 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine source Swiss-Prot : SWS_FT_FI2 117) chain E residue 258 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine source Swiss-Prot : SWS_FT_FI2 118) chain F residue 258 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine source Swiss-Prot : SWS_FT_FI2 119) chain A residue 258 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine source Swiss-Prot : SWS_FT_FI2 120) chain B residue 258 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine source Swiss-Prot : SWS_FT_FI2 121) chain A residue 255-268 type prosite sequence SFSKIFSLYGERVG description AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SFSKifSLyGERVG source prosite : PS00105

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