eF-site ID 1s8a-C PDB Code 1s8a Chain C 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 C:  MELTTRTLPARKHIALVAHDHCKQMLMSWVERHQPLLEQH VLYATGTTGNLISRATGMNVNAMLSGPMGGDQQVGALISE GKIDVLIFFWDPLNAVPQDPDVKALLRLATVWNIPVATNV ATADFIIQSPHFNDAVDILIPDYQRYLADRLK Description Functional site 1) chain C residue 17 type sequence V description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 2) chain C residue 18 type sequence A description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 3) chain C residue 23 type sequence K description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 4) chain C residue 45 type sequence T description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 5) chain C residue 47 type sequence T description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 6) chain C residue 48 type sequence T description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 7) chain C residue 65 type sequence S description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 8) chain C residue 66 type sequence G description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 9) chain C residue 67 type sequence P description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 10) chain C residue 71 type sequence D description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 11) chain C residue 98 type sequence Q description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 12) chain C residue 150 type sequence R description BINDING SITE FOR RESIDUE PGA D 204 source : AC4 13) chain C residue 19 type catalytic sequence H description 85 source MCSA : MCSA3 14) chain C residue 66 type catalytic sequence G description 85 source MCSA : MCSA3 15) chain C residue 71 type catalytic sequence D description 85 source MCSA : MCSA3 16) chain C residue 91 type catalytic sequence D description 85 source MCSA : MCSA3 17) chain C residue 98 type catalytic sequence Q description 85 source MCSA : MCSA3 18) chain C residue 101 type catalytic sequence D description 85 source MCSA : MCSA3 19) chain C residue 107 type catalytic sequence R description 85 source MCSA : MCSA3 20) chain C 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 21) chain C 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 22) chain C 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 23) chain C 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 24) chain C 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 25) chain C 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

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