eF-site ID 5a1a-A PDB Code 5a1a Chain A 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 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 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 A residue 201 type catalytic sequence D description 422 source MCSA : MCSA1 27) chain A residue 604 type catalytic sequence N description 422 source MCSA : MCSA1 28) chain A residue 357 type catalytic sequence H description 422 source MCSA : MCSA1 29) chain A residue 391 type catalytic sequence H description 422 source MCSA : MCSA1 30) chain A residue 416 type catalytic sequence E description 422 source MCSA : MCSA1 31) chain A residue 418 type catalytic sequence H description 422 source MCSA : MCSA1 32) chain A residue 461 type catalytic sequence E description 422 source MCSA : MCSA1 33) chain A residue 537 type catalytic sequence E description 422 source MCSA : MCSA1 34) chain A residue 597 type catalytic sequence N description 422 source MCSA : MCSA1 35) chain A residue 601 type catalytic sequence F description 422 source MCSA : MCSA1 36) 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 37) chain A residue 385-410 type prosite sequence NAVRCSHYPNHPLWYTLCDRYGLYVV description GLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NaVRCSHYPnhplWYtlcDryGLYVV source prosite : PS00719 38) chain A residue 102 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 39) chain A residue 201 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 40) chain A residue 461 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 41) chain A residue 537 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 42) chain A residue 601 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI3 43) chain A residue 604 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 44) chain A residue 999 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI3 45) chain A residue 416 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11045615 source Swiss-Prot : SWS_FT_FI4 46) chain A residue 418 type BINDING sequence H description BINDING => ECO:0000269|PubMed:11045615 source Swiss-Prot : SWS_FT_FI4 47) chain A residue 597 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11045615 source Swiss-Prot : SWS_FT_FI4 48) chain A residue 357 type SITE sequence H description Transition state stabilizer source Swiss-Prot : SWS_FT_FI5 49) chain A residue 391 type SITE sequence H description Transition state stabilizer source Swiss-Prot : SWS_FT_FI5 50) 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 51) chain A residue 461 type ACT_SITE sequence E description Proton donor => ECO:0000269|PubMed:6420154 source Swiss-Prot : SWS_FT_FI1 52) chain A residue 537 type ACT_SITE sequence E description Nucleophile => ECO:0000269|PubMed:1350782 source Swiss-Prot : SWS_FT_FI2

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