eF-site ID 5a1a-B PDB Code 5a1a Chain B click to enlarge 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 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 Description Functional site 1) chain B residue 102 type sequence N description BINDING SITE FOR RESIDUE PTQ B 2001 source : AC6 2) chain B residue 201 type sequence D description BINDING SITE FOR RESIDUE PTQ B 2001 source : AC6 3) chain B residue 502 type sequence M description BINDING SITE FOR RESIDUE PTQ B 2001 source : AC6 4) chain B residue 503 type sequence Y description BINDING SITE FOR RESIDUE PTQ B 2001 source : AC6 5) chain B residue 537 type sequence E description BINDING SITE FOR RESIDUE PTQ B 2001 source : AC6 6) chain B residue 540 type sequence H description BINDING SITE FOR RESIDUE PTQ B 2001 source : AC6 7) chain B residue 598 type sequence D description BINDING SITE FOR RESIDUE PTQ B 2001 source : AC6 8) chain B residue 601 type sequence F description BINDING SITE FOR RESIDUE PTQ B 2001 source : AC6 9) chain B residue 999 type sequence W description BINDING SITE FOR RESIDUE PTQ B 2001 source : AC6 10) chain B residue 416 type sequence E description BINDING SITE FOR RESIDUE MG B 3001 source : AC7 11) chain B residue 418 type sequence H description BINDING SITE FOR RESIDUE MG B 3001 source : AC7 12) chain B residue 461 type sequence E description BINDING SITE FOR RESIDUE MG B 3001 source : AC7 13) chain B residue 15 type sequence D description BINDING SITE FOR RESIDUE MG B 3002 source : AC8 14) chain B residue 18 type sequence N description BINDING SITE FOR RESIDUE MG B 3002 source : AC8 15) chain B residue 21 type sequence V description BINDING SITE FOR RESIDUE MG B 3002 source : AC8 16) chain B residue 161 type sequence Y description BINDING SITE FOR RESIDUE MG B 3002 source : AC8 17) chain B residue 163 type sequence Q description BINDING SITE FOR RESIDUE MG B 3002 source : AC8 18) chain B residue 193 type sequence D description BINDING SITE FOR RESIDUE MG B 3002 source : AC8 19) chain B residue 201 type sequence D description BINDING SITE FOR RESIDUE NA B 4001 source : AC9 20) chain B residue 601 type sequence F description BINDING SITE FOR RESIDUE NA B 4001 source : AC9 21) chain B residue 604 type sequence N description BINDING SITE FOR RESIDUE NA B 4001 source : AC9 22) chain B residue 556 type sequence F description BINDING SITE FOR RESIDUE NA B 4002 source : BC1 23) chain B residue 559 type sequence Y description BINDING SITE FOR RESIDUE NA B 4002 source : BC1 24) chain B residue 560 type sequence P description BINDING SITE FOR RESIDUE NA B 4002 source : BC1 25) chain B residue 562 type sequence L description BINDING SITE FOR RESIDUE NA B 4002 source : BC1 26) chain B residue 201 type catalytic sequence D description 422 source MCSA : MCSA2 27) chain B residue 604 type catalytic sequence N description 422 source MCSA : MCSA2 28) chain B residue 357 type catalytic sequence H description 422 source MCSA : MCSA2 29) chain B residue 391 type catalytic sequence H description 422 source MCSA : MCSA2 30) chain B residue 416 type catalytic sequence E description 422 source MCSA : MCSA2 31) chain B residue 418 type catalytic sequence H description 422 source MCSA : MCSA2 32) chain B residue 461 type catalytic sequence E description 422 source MCSA : MCSA2 33) chain B residue 537 type catalytic sequence E description 422 source MCSA : MCSA2 34) chain B residue 597 type catalytic sequence N description 422 source MCSA : MCSA2 35) chain B residue 601 type catalytic sequence F description 422 source MCSA : MCSA2 36) chain B residue 461 type ACT_SITE sequence E description Proton donor => ECO:0000269|PubMed:6420154 source Swiss-Prot : SWS_FT_FI1 37) chain B residue 537 type ACT_SITE sequence E description Nucleophile => ECO:0000269|PubMed:1350782 source Swiss-Prot : SWS_FT_FI2 38) chain B residue 461 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 39) chain B residue 537 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 40) chain B residue 601 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI3 41) chain B residue 604 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 42) chain B residue 999 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI3 43) chain B residue 102 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 44) chain B residue 201 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 45) chain B residue 416 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11045615 source Swiss-Prot : SWS_FT_FI4 46) chain B residue 418 type BINDING sequence H description BINDING => ECO:0000269|PubMed:11045615 source Swiss-Prot : SWS_FT_FI4 47) chain B residue 597 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11045615 source Swiss-Prot : SWS_FT_FI4 48) chain B residue 357 type SITE sequence H description Transition state stabilizer source Swiss-Prot : SWS_FT_FI5 49) chain B residue 391 type SITE sequence H description Transition state stabilizer source Swiss-Prot : SWS_FT_FI5 50) 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

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