eF-site ID 1s8a-E PDB Code 1s8a Chain E 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 E:  MELTTRTLPARKHIALVAHDHCKQMLMSWVERHQPLLEQH VLYATGTTGNLISRATGMNVNAMLSGPMGGDQQVGALISE GKIDVLIFFWDPLNAVPQDPDVKALLRLATVWNIPVATNV ATADFIIQSPHFNDAVDILIPDYQRYLADRL Description Functional site 1) chain E residue 150 type sequence R description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 2) chain E residue 17 type sequence V description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 3) chain E residue 18 type sequence A description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 4) chain E residue 23 type sequence K description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 5) chain E residue 45 type sequence T description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 6) chain E residue 47 type sequence T description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 7) chain E residue 48 type sequence T description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 8) chain E residue 65 type sequence S description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 9) chain E residue 66 type sequence G description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 10) chain E residue 67 type sequence P description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 11) chain E residue 71 type sequence D description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 12) chain E residue 98 type sequence Q description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 13) chain E residue 19 type catalytic sequence H description 85 source MCSA : MCSA5 14) chain E residue 66 type catalytic sequence G description 85 source MCSA : MCSA5 15) chain E residue 71 type catalytic sequence D description 85 source MCSA : MCSA5 16) chain E residue 91 type catalytic sequence D description 85 source MCSA : MCSA5 17) chain E residue 98 type catalytic sequence Q description 85 source MCSA : MCSA5 18) chain E residue 101 type catalytic sequence D description 85 source MCSA : MCSA5 19) chain E residue 107 type catalytic sequence R description 85 source MCSA : MCSA5 20) chain E 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 E 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 E 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 E 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 E 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 E 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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