eF-site ID 1s8a-F PDB Code 1s8a Chain F click to enlarge Title H98Q Mutant of Methylglyoxal Synthase from E. coli complexed with Phosphoglycolic Acid Classification LYASE Compound Methylglyoxal synthase Source Escherichia coli (strain K12) (MGSA_ECOLI) Sequence F:  MELTTRTLPARKHIALVAHDHCKQMLMSWVERHQPLLEQH VLYATGTTGNLISRATGMNVNAMLSGPMGGDQQVGALISE GKIDVLIFFWDPLNAVPQDPDVKALLRLATVWNIPVATNV ATADFIIQSPHFNDAVDILIPDYQRYLADRLK Description Functional site 1) chain F residue 150 type sequence R description BINDING SITE FOR RESIDUE PGA A 201 source : AC1 2) chain F residue 17 type sequence V description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 3) chain F residue 18 type sequence A description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 4) chain F residue 23 type sequence K description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 5) chain F residue 45 type sequence T description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 6) chain F residue 47 type sequence T description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 7) chain F residue 48 type sequence T description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 8) chain F residue 65 type sequence S description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 9) chain F residue 66 type sequence G description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 10) chain F residue 67 type sequence P description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 11) chain F residue 71 type sequence D description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 12) chain F residue 98 type sequence Q description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 13) chain F residue 19 type catalytic sequence H description 85 source MCSA : MCSA6 14) chain F residue 66 type catalytic sequence G description 85 source MCSA : MCSA6 15) chain F residue 71 type catalytic sequence D description 85 source MCSA : MCSA6 16) chain F residue 91 type catalytic sequence D description 85 source MCSA : MCSA6 17) chain F residue 98 type catalytic sequence Q description 85 source MCSA : MCSA6 18) chain F residue 101 type catalytic sequence D description 85 source MCSA : MCSA6 19) chain F residue 107 type catalytic sequence R description 85 source MCSA : MCSA6 20) chain F residue 71 type ACT_SITE sequence D description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00549, ECO:0000269|PubMed:10715115, ECO:0000269|PubMed:11389594, ECO:0000269|PubMed:15049687, ECO:0000269|PubMed:9665712 source Swiss-Prot : SWS_FT_FI1 21) chain F residue 19 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00549, ECO:0000269|PubMed:11389594, ECO:0007744|PDB:1IK4 source Swiss-Prot : SWS_FT_FI2 22) chain F residue 23 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00549, ECO:0000269|PubMed:10715115, ECO:0000269|PubMed:11389594, ECO:0000269|PubMed:15049687, ECO:0007744|PDB:1EGH, ECO:0007744|PDB:1IK4, ECO:0007744|PDB:1S89, ECO:0007744|PDB:1S8A source Swiss-Prot : SWS_FT_FI3 23) chain F residue 45 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00549, ECO:0000269|PubMed:10715115, ECO:0000269|PubMed:11389594, ECO:0000269|PubMed:15049687, ECO:0007744|PDB:1EGH, ECO:0007744|PDB:1IK4, ECO:0007744|PDB:1S89, ECO:0007744|PDB:1S8A source Swiss-Prot : SWS_FT_FI3 24) chain F residue 65 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00549, ECO:0000269|PubMed:10715115, ECO:0000269|PubMed:11389594, ECO:0000269|PubMed:15049687, ECO:0007744|PDB:1EGH, ECO:0007744|PDB:1IK4, ECO:0007744|PDB:1S89, ECO:0007744|PDB:1S8A source Swiss-Prot : SWS_FT_FI3 25) chain F residue 98 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_00549, ECO:0000269|PubMed:10715115, ECO:0000269|PubMed:11389594, ECO:0007744|PDB:1EGH, ECO:0007744|PDB:1IK4 source Swiss-Prot : SWS_FT_FI4

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