eF-site ID 1s8a-A PDB Code 1s8a Chain A click to enlarge Title H98Q Mutant of Methylglyoxal Synthase from E. coli complexed with Phosphoglycolic Acid Classification LYASE Compound Methylglyoxal synthase Source null (MGSA_ECOLI) Sequence A:  MELTTRTLPARKHIALVAHDHCKQMLMSWVERHQPLLEQH VLYATGTTGNLISRATGMNVNAMLSGPMGGDQQVGALISE GKIDVLIFFWDPLNAVPQDPDVKALLRLATVWNIPVATNV ATADFIIQSPHFNDAVDILIPDYQRYLADRLK Description Functional site 1) chain A residue 17 type sequence V description BINDING SITE FOR RESIDUE PGA A 201 source : AC1 2) chain A residue 18 type sequence A description BINDING SITE FOR RESIDUE PGA A 201 source : AC1 3) chain A residue 23 type sequence K description BINDING SITE FOR RESIDUE PGA A 201 source : AC1 4) chain A residue 45 type sequence T description BINDING SITE FOR RESIDUE PGA A 201 source : AC1 5) chain A residue 47 type sequence T description BINDING SITE FOR RESIDUE PGA A 201 source : AC1 6) chain A residue 48 type sequence T description BINDING SITE FOR RESIDUE PGA A 201 source : AC1 7) chain A residue 65 type sequence S description BINDING SITE FOR RESIDUE PGA A 201 source : AC1 8) chain A residue 66 type sequence G description BINDING SITE FOR RESIDUE PGA A 201 source : AC1 9) chain A residue 67 type sequence P description BINDING SITE FOR RESIDUE PGA A 201 source : AC1 10) chain A residue 71 type sequence D description BINDING SITE FOR RESIDUE PGA A 201 source : AC1 11) chain A residue 98 type sequence Q description BINDING SITE FOR RESIDUE PGA A 201 source : AC1 12) chain A residue 150 type sequence R description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 13) chain A 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 14) chain A 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 15) chain A 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 16) chain A 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 17) chain A 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 18) chain A 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 19) chain A residue 19 type catalytic sequence H description 85 source MCSA : MCSA1 20) chain A residue 66 type catalytic sequence G description 85 source MCSA : MCSA1 21) chain A residue 71 type catalytic sequence D description 85 source MCSA : MCSA1 22) chain A residue 91 type catalytic sequence D description 85 source MCSA : MCSA1 23) chain A residue 98 type catalytic sequence Q description 85 source MCSA : MCSA1 24) chain A residue 101 type catalytic sequence D description 85 source MCSA : MCSA1 25) chain A residue 107 type catalytic sequence R description 85 source MCSA : MCSA1 26) chain A residue 65-73 type prosite sequence SGPMGGDQQ description METHYLGLYOXAL_SYNTH Methylglyoxal synthase active site. SGPMGGDqQ source prosite : PS01335

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