eF-site ID 5a1a-ABCD PDB Code 5a1a Chain A, B, C, D Title 2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor Classification HYDROLASE Compound BETA-GALACTOSIDASE Source ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12; Sequence A:  MITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEE ARTDRPSQQLRSLNGEWRFAWFPAPEAVPESWLECDLPEA DTVVVPSNWQMHGYDAPIYTNVTYPITVNPPFVPTENPTG CYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWVGY GQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQD MWRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAVLE AEVQMCGELRDYLRVTVSLWQGETQVASGTAPFGGEIIDE RGGYADRVTLRLNVENPKLWSAEIPNLYRAVVELHTADGT LIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHEHHP LHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTL CDRYGLYVVDEANIETHGMVPMNRLTDDPRWLPAMSERVT RMVQRDRNHPSVIIWSLGNESGHGANHDALYRWIKSVDPS RPVQYEGGGADTTATDIICPMYARVDEDQPFPAVPKWSIK KWLSLPGETRPLILCEYAHAMGNSLGGFAKYWQAFRQYPR LQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQF CMNGLVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSE YLFRHSDNELLHWMVALDGKPLASGEVPLDVAPQGKQLIE LPELPQPESAGQLWLTVRVVQPNATAWSEAGHISAWQQWR LAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQFNRQ SGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVSEATRI DPNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTAHA WQHQGKTLFISRKTYRIDGSGQMAITVDVEVASDTPHPAR IGLNCQLAQVAERVNWLGLGPQENYPDRLTAACFDRWDLP LSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNISR YSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSP SVSAEFQLSAGRYHYQLVWCQK B:  MITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEE ARTDRPSQQLRSLNGEWRFAWFPAPEAVPESWLECDLPEA DTVVVPSNWQMHGYDAPIYTNVTYPITVNPPFVPTENPTG CYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWVGY GQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQD MWRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAVLE AEVQMCGELRDYLRVTVSLWQGETQVASGTAPFGGEIIDE RGGYADRVTLRLNVENPKLWSAEIPNLYRAVVELHTADGT LIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHEHHP LHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTL CDRYGLYVVDEANIETHGMVPMNRLTDDPRWLPAMSERVT RMVQRDRNHPSVIIWSLGNESGHGANHDALYRWIKSVDPS RPVQYEGGGADTTATDIICPMYARVDEDQPFPAVPKWSIK KWLSLPGETRPLILCEYAHAMGNSLGGFAKYWQAFRQYPR LQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQF CMNGLVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSE YLFRHSDNELLHWMVALDGKPLASGEVPLDVAPQGKQLIE LPELPQPESAGQLWLTVRVVQPNATAWSEAGHISAWQQWR LAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQFNRQ SGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVSEATRI DPNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTAHA WQHQGKTLFISRKTYRIDGSGQMAITVDVEVASDTPHPAR IGLNCQLAQVAERVNWLGLGPQENYPDRLTAACFDRWDLP LSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNISR YSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSP SVSAEFQLSAGRYHYQLVWCQK C:  MITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEE ARTDRPSQQLRSLNGEWRFAWFPAPEAVPESWLECDLPEA DTVVVPSNWQMHGYDAPIYTNVTYPITVNPPFVPTENPTG CYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWVGY GQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQD MWRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAVLE AEVQMCGELRDYLRVTVSLWQGETQVASGTAPFGGEIIDE RGGYADRVTLRLNVENPKLWSAEIPNLYRAVVELHTADGT LIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHEHHP LHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTL CDRYGLYVVDEANIETHGMVPMNRLTDDPRWLPAMSERVT RMVQRDRNHPSVIIWSLGNESGHGANHDALYRWIKSVDPS RPVQYEGGGADTTATDIICPMYARVDEDQPFPAVPKWSIK KWLSLPGETRPLILCEYAHAMGNSLGGFAKYWQAFRQYPR LQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQF CMNGLVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSE YLFRHSDNELLHWMVALDGKPLASGEVPLDVAPQGKQLIE LPELPQPESAGQLWLTVRVVQPNATAWSEAGHISAWQQWR LAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQFNRQ SGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVSEATRI DPNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTAHA WQHQGKTLFISRKTYRIDGSGQMAITVDVEVASDTPHPAR IGLNCQLAQVAERVNWLGLGPQENYPDRLTAACFDRWDLP LSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNISR YSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSP SVSAEFQLSAGRYHYQLVWCQK D:  MITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEE ARTDRPSQQLRSLNGEWRFAWFPAPEAVPESWLECDLPEA DTVVVPSNWQMHGYDAPIYTNVTYPITVNPPFVPTENPTG CYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWVGY GQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQD MWRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAVLE AEVQMCGELRDYLRVTVSLWQGETQVASGTAPFGGEIIDE RGGYADRVTLRLNVENPKLWSAEIPNLYRAVVELHTADGT LIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHEHHP LHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTL CDRYGLYVVDEANIETHGMVPMNRLTDDPRWLPAMSERVT RMVQRDRNHPSVIIWSLGNESGHGANHDALYRWIKSVDPS RPVQYEGGGADTTATDIICPMYARVDEDQPFPAVPKWSIK KWLSLPGETRPLILCEYAHAMGNSLGGFAKYWQAFRQYPR LQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQF CMNGLVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSE YLFRHSDNELLHWMVALDGKPLASGEVPLDVAPQGKQLIE LPELPQPESAGQLWLTVRVVQPNATAWSEAGHISAWQQWR LAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQFNRQ SGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVSEATRI DPNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTAHA WQHQGKTLFISRKTYRIDGSGQMAITVDVEVASDTPHPAR IGLNCQLAQVAERVNWLGLGPQENYPDRLTAACFDRWDLP LSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNISR YSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSP SVSAEFQLSAGRYHYQLVWCQK Description (1)  BETA-GALACTOSIDASE (E.C.3.2.1.23) Functional site 1) chain A residue 102 type sequence N description BINDING SITE FOR RESIDUE PTQ A 2001 source : AC1 2) chain A residue 201 type sequence D description BINDING SITE FOR RESIDUE PTQ A 2001 source : AC1 3) chain A residue 502 type sequence M description BINDING SITE FOR RESIDUE PTQ A 2001 source : AC1 4) chain A residue 503 type sequence Y description BINDING SITE FOR RESIDUE PTQ A 2001 source : AC1 5) chain A residue 537 type sequence E description BINDING SITE FOR RESIDUE PTQ A 2001 source : AC1 6) chain A residue 540 type sequence H description BINDING SITE FOR RESIDUE PTQ A 2001 source : AC1 7) chain A residue 598 type sequence D description BINDING SITE FOR RESIDUE PTQ A 2001 source : AC1 8) chain A residue 601 type sequence F description BINDING SITE FOR RESIDUE PTQ A 2001 source : AC1 9) chain A residue 999 type sequence W description BINDING SITE FOR RESIDUE PTQ A 2001 source : AC1 10) chain A residue 416 type sequence E description BINDING SITE FOR RESIDUE MG A 3001 source : AC2 11) chain A residue 418 type sequence H description BINDING SITE FOR RESIDUE MG A 3001 source : AC2 12) chain A residue 461 type sequence E description BINDING SITE FOR RESIDUE MG A 3001 source : AC2 13) chain A residue 15 type sequence D description BINDING SITE FOR RESIDUE MG A 3002 source : AC3 14) chain A residue 18 type sequence N description BINDING SITE FOR RESIDUE MG A 3002 source : AC3 15) chain A residue 21 type sequence V description BINDING SITE FOR RESIDUE MG A 3002 source : AC3 16) chain A residue 161 type sequence Y description BINDING SITE FOR RESIDUE MG A 3002 source : AC3 17) chain A residue 163 type sequence Q description BINDING SITE FOR RESIDUE MG A 3002 source : AC3 18) chain A residue 193 type sequence D description BINDING SITE FOR RESIDUE MG A 3002 source : AC3 19) chain A residue 201 type sequence D description BINDING SITE FOR RESIDUE NA A 4001 source : AC4 20) chain A residue 601 type sequence F description BINDING SITE FOR RESIDUE NA A 4001 source : AC4 21) chain A residue 604 type sequence N description BINDING SITE FOR RESIDUE NA A 4001 source : AC4 22) chain A residue 556 type sequence F description BINDING SITE FOR RESIDUE NA A 4002 source : AC5 23) chain A residue 559 type sequence Y description BINDING SITE FOR RESIDUE NA A 4002 source : AC5 24) chain A residue 560 type sequence P description BINDING SITE FOR RESIDUE NA A 4002 source : AC5 25) chain A residue 562 type sequence L description BINDING SITE FOR RESIDUE NA A 4002 source : AC5 26) chain B residue 102 type sequence N description BINDING SITE FOR RESIDUE PTQ B 2001 source : AC6 27) chain B residue 201 type sequence D description BINDING SITE FOR RESIDUE PTQ B 2001 source : AC6 28) chain B residue 502 type sequence M description BINDING SITE FOR RESIDUE PTQ B 2001 source : AC6 29) chain B residue 503 type sequence Y description BINDING SITE FOR RESIDUE PTQ B 2001 source : AC6 30) chain B residue 537 type sequence E description BINDING SITE FOR RESIDUE PTQ B 2001 source : AC6 31) chain B residue 540 type sequence H description BINDING SITE FOR RESIDUE PTQ B 2001 source : AC6 32) chain B residue 598 type sequence D description BINDING SITE FOR RESIDUE PTQ B 2001 source : AC6 33) chain B residue 601 type sequence F description BINDING SITE FOR RESIDUE PTQ B 2001 source : AC6 34) chain B residue 999 type sequence W description BINDING SITE FOR RESIDUE PTQ B 2001 source : AC6 35) chain B residue 416 type sequence E description BINDING SITE FOR RESIDUE MG B 3001 source : AC7 36) chain B residue 418 type sequence H description BINDING SITE FOR RESIDUE MG B 3001 source : AC7 37) chain B residue 461 type sequence E description BINDING SITE FOR RESIDUE MG B 3001 source : AC7 38) chain B residue 15 type sequence D description BINDING SITE FOR RESIDUE MG B 3002 source : AC8 39) chain B residue 18 type sequence N description BINDING SITE FOR RESIDUE MG B 3002 source : AC8 40) chain B residue 21 type sequence V description BINDING SITE FOR RESIDUE MG B 3002 source : AC8 41) chain B residue 161 type sequence Y description BINDING SITE FOR RESIDUE MG B 3002 source : AC8 42) chain B residue 163 type sequence Q description BINDING SITE FOR RESIDUE MG B 3002 source : AC8 43) chain B residue 193 type sequence D description BINDING SITE FOR RESIDUE MG B 3002 source : AC8 44) chain B residue 201 type sequence D description BINDING SITE FOR RESIDUE NA B 4001 source : AC9 45) chain B residue 601 type sequence F description BINDING SITE FOR RESIDUE NA B 4001 source : AC9 46) chain B residue 604 type sequence N description BINDING SITE FOR RESIDUE NA B 4001 source : AC9 47) chain B residue 556 type sequence F description BINDING SITE FOR RESIDUE NA B 4002 source : BC1 48) chain B residue 559 type sequence Y description BINDING SITE FOR RESIDUE NA B 4002 source : BC1 49) chain B residue 560 type sequence P description BINDING SITE FOR RESIDUE NA B 4002 source : BC1 50) chain B residue 562 type sequence L description BINDING SITE FOR RESIDUE NA B 4002 source : BC1 51) chain C residue 102 type sequence N description BINDING SITE FOR RESIDUE PTQ C 2001 source : BC2 52) chain C residue 201 type sequence D description BINDING SITE FOR RESIDUE PTQ C 2001 source : BC2 53) chain C residue 502 type sequence M description BINDING SITE FOR RESIDUE PTQ C 2001 source : BC2 54) chain C residue 503 type sequence Y description BINDING SITE FOR RESIDUE PTQ C 2001 source : BC2 55) chain C residue 537 type sequence E description BINDING SITE FOR RESIDUE PTQ C 2001 source : BC2 56) chain C residue 540 type sequence H description BINDING SITE FOR RESIDUE PTQ C 2001 source : BC2 57) chain C residue 598 type sequence D description BINDING SITE FOR RESIDUE PTQ C 2001 source : BC2 58) chain C residue 601 type sequence F description BINDING SITE FOR RESIDUE PTQ C 2001 source : BC2 59) chain C residue 999 type sequence W description BINDING SITE FOR RESIDUE PTQ C 2001 source : BC2 60) chain C residue 416 type sequence E description BINDING SITE FOR RESIDUE MG C 3001 source : BC3 61) chain C residue 418 type sequence H description BINDING SITE FOR RESIDUE MG C 3001 source : BC3 62) chain C residue 461 type sequence E description BINDING SITE FOR RESIDUE MG C 3001 source : BC3 63) chain C residue 15 type sequence D description BINDING SITE FOR RESIDUE MG C 3002 source : BC4 64) chain C residue 18 type sequence N description BINDING SITE FOR RESIDUE MG C 3002 source : BC4 65) chain C residue 21 type sequence V description BINDING SITE FOR RESIDUE MG C 3002 source : BC4 66) chain C residue 161 type sequence Y description BINDING SITE FOR RESIDUE MG C 3002 source : BC4 67) chain C residue 163 type sequence Q description BINDING SITE FOR RESIDUE MG C 3002 source : BC4 68) chain C residue 193 type sequence D description BINDING SITE FOR RESIDUE MG C 3002 source : BC4 69) chain C residue 201 type sequence D description BINDING SITE FOR RESIDUE NA C 4001 source : BC5 70) chain C residue 601 type sequence F description BINDING SITE FOR RESIDUE NA C 4001 source : BC5 71) chain C residue 604 type sequence N description BINDING SITE FOR RESIDUE NA C 4001 source : BC5 72) chain C residue 556 type sequence F description BINDING SITE FOR RESIDUE NA C 4002 source : BC6 73) chain C residue 559 type sequence Y description BINDING SITE FOR RESIDUE NA C 4002 source : BC6 74) chain C residue 560 type sequence P description BINDING SITE FOR RESIDUE NA C 4002 source : BC6 75) chain C residue 562 type sequence L description BINDING SITE FOR RESIDUE NA C 4002 source : BC6 76) chain D residue 102 type sequence N description BINDING SITE FOR RESIDUE PTQ D 2001 source : BC7 77) chain D residue 201 type sequence D description BINDING SITE FOR RESIDUE PTQ D 2001 source : BC7 78) chain D residue 502 type sequence M description BINDING SITE FOR RESIDUE PTQ D 2001 source : BC7 79) chain D residue 503 type sequence Y description BINDING SITE FOR RESIDUE PTQ D 2001 source : BC7 80) chain D residue 537 type sequence E description BINDING SITE FOR RESIDUE PTQ D 2001 source : BC7 81) chain D residue 540 type sequence H description BINDING SITE FOR RESIDUE PTQ D 2001 source : BC7 82) chain D residue 598 type sequence D description BINDING SITE FOR RESIDUE PTQ D 2001 source : BC7 83) chain D residue 601 type sequence F description BINDING SITE FOR RESIDUE PTQ D 2001 source : BC7 84) chain D residue 999 type sequence W description BINDING SITE FOR RESIDUE PTQ D 2001 source : BC7 85) chain D residue 416 type sequence E description BINDING SITE FOR RESIDUE MG D 3001 source : BC8 86) chain D residue 418 type sequence H description BINDING SITE FOR RESIDUE MG D 3001 source : BC8 87) chain D residue 461 type sequence E description BINDING SITE FOR RESIDUE MG D 3001 source : BC8 88) chain D residue 15 type sequence D description BINDING SITE FOR RESIDUE MG D 3002 source : BC9 89) chain D residue 18 type sequence N description BINDING SITE FOR RESIDUE MG D 3002 source : BC9 90) chain D residue 21 type sequence V description BINDING SITE FOR RESIDUE MG D 3002 source : BC9 91) chain D residue 161 type sequence Y description BINDING SITE FOR RESIDUE MG D 3002 source : BC9 92) chain D residue 163 type sequence Q description BINDING SITE FOR RESIDUE MG D 3002 source : BC9 93) chain D residue 193 type sequence D description BINDING SITE FOR RESIDUE MG D 3002 source : BC9 94) chain D residue 201 type sequence D description BINDING SITE FOR RESIDUE NA D 4001 source : CC1 95) chain D residue 601 type sequence F description BINDING SITE FOR RESIDUE NA D 4001 source : CC1 96) chain D residue 604 type sequence N description BINDING SITE FOR RESIDUE NA D 4001 source : CC1 97) chain D residue 556 type sequence F description BINDING SITE FOR RESIDUE NA D 4002 source : CC2 98) chain D residue 559 type sequence Y description BINDING SITE FOR RESIDUE NA D 4002 source : CC2 99) chain D residue 560 type sequence P description BINDING SITE FOR RESIDUE NA D 4002 source : CC2 100) chain D residue 562 type sequence L description BINDING SITE FOR RESIDUE NA D 4002 source : CC2 101) chain A residue 201 type catalytic sequence D description 422 source MCSA : MCSA1 102) chain A residue 604 type catalytic sequence N description 422 source MCSA : MCSA1 103) chain A residue 357 type catalytic sequence H description 422 source MCSA : MCSA1 104) chain A residue 391 type catalytic sequence H description 422 source MCSA : MCSA1 105) chain A residue 416 type catalytic sequence E description 422 source MCSA : MCSA1 106) chain A residue 418 type catalytic sequence H description 422 source MCSA : MCSA1 107) chain A residue 461 type catalytic sequence E description 422 source MCSA : MCSA1 108) chain A residue 537 type catalytic sequence E description 422 source MCSA : MCSA1 109) chain A residue 597 type catalytic sequence N description 422 source MCSA : MCSA1 110) chain A residue 601 type catalytic sequence F description 422 source MCSA : MCSA1 111) chain B residue 201 type catalytic sequence D description 422 source MCSA : MCSA2 112) chain B residue 604 type catalytic sequence N description 422 source MCSA : MCSA2 113) chain B residue 357 type catalytic sequence H description 422 source MCSA : MCSA2 114) chain B residue 391 type catalytic sequence H description 422 source MCSA : MCSA2 115) chain B residue 416 type catalytic sequence E description 422 source MCSA : MCSA2 116) chain B residue 418 type catalytic sequence H description 422 source MCSA : MCSA2 117) chain B residue 461 type catalytic sequence E description 422 source MCSA : MCSA2 118) chain B residue 537 type catalytic sequence E description 422 source MCSA : MCSA2 119) chain B residue 597 type catalytic sequence N description 422 source MCSA : MCSA2 120) chain B residue 601 type catalytic sequence F description 422 source MCSA : MCSA2 121) chain C residue 201 type catalytic sequence D description 422 source MCSA : MCSA3 122) chain C residue 604 type catalytic sequence N description 422 source MCSA : MCSA3 123) chain C residue 357 type catalytic sequence H description 422 source MCSA : MCSA3 124) chain C residue 391 type catalytic sequence H description 422 source MCSA : MCSA3 125) chain C residue 416 type catalytic sequence E description 422 source MCSA : MCSA3 126) chain C residue 418 type catalytic sequence H description 422 source MCSA : MCSA3 127) chain C residue 461 type catalytic sequence E description 422 source MCSA : MCSA3 128) chain C residue 537 type catalytic sequence E description 422 source MCSA : MCSA3 129) chain C residue 597 type catalytic sequence N description 422 source MCSA : MCSA3 130) chain C residue 601 type catalytic sequence F description 422 source MCSA : MCSA3 131) chain D residue 201 type catalytic sequence D description 422 source MCSA : MCSA4 132) chain D residue 604 type catalytic sequence N description 422 source MCSA : MCSA4 133) chain D residue 357 type catalytic sequence H description 422 source MCSA : MCSA4 134) chain D residue 391 type catalytic sequence H description 422 source MCSA : MCSA4 135) chain D residue 416 type catalytic sequence E description 422 source MCSA : MCSA4 136) chain D residue 418 type catalytic sequence H description 422 source MCSA : MCSA4 137) chain D residue 461 type catalytic sequence E description 422 source MCSA : MCSA4 138) chain D residue 537 type catalytic sequence E description 422 source MCSA : MCSA4 139) chain D residue 597 type catalytic sequence N description 422 source MCSA : MCSA4 140) chain D residue 601 type catalytic sequence F description 422 source MCSA : MCSA4 141) chain A residue 447-461 type prosite sequence DRNHPSVIIWSLGNE description GLYCOSYL_HYDROL_F2_2 Glycosyl hydrolases family 2 acid/base catalyst. DRNHPSVIIWSlg.NE source prosite : PS00608 142) chain A residue 385-410 type prosite sequence NAVRCSHYPNHPLWYTLCDRYGLYVV description GLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NaVRCSHYPnhplWYtlcDryGLYVV source prosite : PS00719 143) chain A residue 102 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 144) chain B residue 461 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 145) chain B residue 537 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 146) chain B residue 601 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI3 147) chain B residue 604 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 148) chain B residue 999 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI3 149) chain C residue 102 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 150) chain C residue 201 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 151) chain C residue 461 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 152) chain C residue 537 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 153) chain C residue 601 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI3 154) chain A residue 201 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 155) chain C residue 604 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 156) chain C residue 999 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI3 157) chain D residue 102 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 158) chain D residue 201 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 159) chain D residue 461 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 160) chain D residue 537 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 161) chain D residue 601 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI3 162) chain D residue 604 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 163) chain D residue 999 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI3 164) chain A residue 461 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 165) chain A residue 537 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 166) chain A residue 601 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI3 167) chain A residue 604 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 168) chain A residue 999 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI3 169) chain B residue 102 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 170) chain B residue 201 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 171) chain A residue 416 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11045615 source Swiss-Prot : SWS_FT_FI4 172) chain D residue 416 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11045615 source Swiss-Prot : SWS_FT_FI4 173) chain D residue 418 type BINDING sequence H description BINDING => ECO:0000269|PubMed:11045615 source Swiss-Prot : SWS_FT_FI4 174) chain D residue 597 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11045615 source Swiss-Prot : SWS_FT_FI4 175) chain A residue 418 type BINDING sequence H description BINDING => ECO:0000269|PubMed:11045615 source Swiss-Prot : SWS_FT_FI4 176) chain A residue 597 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11045615 source Swiss-Prot : SWS_FT_FI4 177) chain B residue 416 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11045615 source Swiss-Prot : SWS_FT_FI4 178) chain B residue 418 type BINDING sequence H description BINDING => ECO:0000269|PubMed:11045615 source Swiss-Prot : SWS_FT_FI4 179) chain B residue 597 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11045615 source Swiss-Prot : SWS_FT_FI4 180) chain C residue 416 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11045615 source Swiss-Prot : SWS_FT_FI4 181) chain C residue 418 type BINDING sequence H description BINDING => ECO:0000269|PubMed:11045615 source Swiss-Prot : SWS_FT_FI4 182) chain C residue 597 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11045615 source Swiss-Prot : SWS_FT_FI4 183) chain A residue 357 type SITE sequence H description Transition state stabilizer source Swiss-Prot : SWS_FT_FI5 184) chain A residue 391 type SITE sequence H description Transition state stabilizer source Swiss-Prot : SWS_FT_FI5 185) chain B residue 357 type SITE sequence H description Transition state stabilizer source Swiss-Prot : SWS_FT_FI5 186) chain B residue 391 type SITE sequence H description Transition state stabilizer source Swiss-Prot : SWS_FT_FI5 187) chain C residue 357 type SITE sequence H description Transition state stabilizer source Swiss-Prot : SWS_FT_FI5 188) chain C residue 391 type SITE sequence H description Transition state stabilizer source Swiss-Prot : SWS_FT_FI5 189) chain D residue 357 type SITE sequence H description Transition state stabilizer source Swiss-Prot : SWS_FT_FI5 190) chain D residue 391 type SITE sequence H description Transition state stabilizer source Swiss-Prot : SWS_FT_FI5 191) chain A residue 999 type SITE sequence W description Important for ensuring that an appropriate proportion of lactose is converted to allolactose source Swiss-Prot : SWS_FT_FI6 192) chain B residue 999 type SITE sequence W description Important for ensuring that an appropriate proportion of lactose is converted to allolactose source Swiss-Prot : SWS_FT_FI6 193) chain C residue 999 type SITE sequence W description Important for ensuring that an appropriate proportion of lactose is converted to allolactose source Swiss-Prot : SWS_FT_FI6 194) chain D residue 999 type SITE sequence W description Important for ensuring that an appropriate proportion of lactose is converted to allolactose source Swiss-Prot : SWS_FT_FI6 195) chain A residue 461 type ACT_SITE sequence E description Proton donor => ECO:0000269|PubMed:6420154 source Swiss-Prot : SWS_FT_FI1 196) chain B residue 461 type ACT_SITE sequence E description Proton donor => ECO:0000269|PubMed:6420154 source Swiss-Prot : SWS_FT_FI1 197) chain C residue 461 type ACT_SITE sequence E description Proton donor => ECO:0000269|PubMed:6420154 source Swiss-Prot : SWS_FT_FI1 198) chain D residue 461 type ACT_SITE sequence E description Proton donor => ECO:0000269|PubMed:6420154 source Swiss-Prot : SWS_FT_FI1 199) chain A residue 537 type ACT_SITE sequence E description Nucleophile => ECO:0000269|PubMed:1350782 source Swiss-Prot : SWS_FT_FI2 200) chain B residue 537 type ACT_SITE sequence E description Nucleophile => ECO:0000269|PubMed:1350782 source Swiss-Prot : SWS_FT_FI2 201) chain C residue 537 type ACT_SITE sequence E description Nucleophile => ECO:0000269|PubMed:1350782 source Swiss-Prot : SWS_FT_FI2 202) chain D residue 537 type ACT_SITE sequence E description Nucleophile => ECO:0000269|PubMed:1350782 source Swiss-Prot : SWS_FT_FI2

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