eF-site ID 1s8a-B PDB Code 1s8a Chain B 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 B:  MELTTRTLPARKHIALVAHDHCKQMLMSWVERHQPLLEQH VLYATGTTGNLISRATGMNVNAMLSGPMGGDQQVGALISE GKIDVLIFFWDPLNAVPQDPDVKALLRLATVWNIPVATNV ATADFIIQSPHFNDAVDILIPDYQRYLADRLK Description Functional site 1) chain B residue 17 type sequence V description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 2) chain B residue 18 type sequence A description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 3) chain B residue 23 type sequence K description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 4) chain B residue 45 type sequence T description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 5) chain B residue 47 type sequence T description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 6) chain B residue 48 type sequence T description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 7) chain B residue 65 type sequence S description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 8) chain B residue 66 type sequence G description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 9) chain B residue 67 type sequence P description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 10) chain B residue 71 type sequence D description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 11) chain B residue 150 type sequence R description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 12) chain B residue 19 type catalytic sequence H description 85 source MCSA : MCSA2 13) chain B residue 66 type catalytic sequence G description 85 source MCSA : MCSA2 14) chain B residue 71 type catalytic sequence D description 85 source MCSA : MCSA2 15) chain B residue 91 type catalytic sequence D description 85 source MCSA : MCSA2 16) chain B residue 98 type catalytic sequence Q description 85 source MCSA : MCSA2 17) chain B residue 101 type catalytic sequence D description 85 source MCSA : MCSA2 18) chain B residue 107 type catalytic sequence R description 85 source MCSA : MCSA2 19) chain B 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 20) chain B 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 B 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 B 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 B 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 B 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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