eF-site ID 1s8a-ABCDEF PDB Code 1s8a Chain A, B, C, D, E, 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 A:  MELTTRTLPARKHIALVAHDHCKQMLMSWVERHQPLLEQH VLYATGTTGNLISRATGMNVNAMLSGPMGGDQQVGALISE GKIDVLIFFWDPLNAVPQDPDVKALLRLATVWNIPVATNV ATADFIIQSPHFNDAVDILIPDYQRYLADRLK B:  MELTTRTLPARKHIALVAHDHCKQMLMSWVERHQPLLEQH VLYATGTTGNLISRATGMNVNAMLSGPMGGDQQVGALISE GKIDVLIFFWDPLNAVPQDPDVKALLRLATVWNIPVATNV ATADFIIQSPHFNDAVDILIPDYQRYLADRLK C:  MELTTRTLPARKHIALVAHDHCKQMLMSWVERHQPLLEQH VLYATGTTGNLISRATGMNVNAMLSGPMGGDQQVGALISE GKIDVLIFFWDPLNAVPQDPDVKALLRLATVWNIPVATNV ATADFIIQSPHFNDAVDILIPDYQRYLADRLK D:  MELTTRTLPARKHIALVAHDHCKQMLMSWVERHQPLLEQH VLYATGTTGNLISRATGMNVNAMLSGPMGGDQQVGALISE GKIDVLIFFWDPLNAVPQDPDVKALLRLATVWNIPVATNV ATADFIIQSPHFNDAVDILIPDYQRYLADRL E:  MELTTRTLPARKHIALVAHDHCKQMLMSWVERHQPLLEQH VLYATGTTGNLISRATGMNVNAMLSGPMGGDQQVGALISE GKIDVLIFFWDPLNAVPQDPDVKALLRLATVWNIPVATNV ATADFIIQSPHFNDAVDILIPDYQRYLADRL F:  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 F residue 150 type sequence R description BINDING SITE FOR RESIDUE PGA A 201 source : AC1 13) chain B residue 17 type sequence V description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 14) chain B residue 18 type sequence A description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 15) chain B residue 23 type sequence K description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 16) chain B residue 45 type sequence T description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 17) chain B residue 47 type sequence T description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 18) chain B residue 48 type sequence T description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 19) chain B residue 65 type sequence S description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 20) chain B residue 66 type sequence G description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 21) chain B residue 67 type sequence P description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 22) chain B residue 71 type sequence D description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 23) chain E residue 150 type sequence R description BINDING SITE FOR RESIDUE PGA B 202 source : AC2 24) chain C residue 17 type sequence V description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 25) chain C residue 18 type sequence A description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 26) chain C residue 23 type sequence K description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 27) chain C residue 45 type sequence T description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 28) chain C residue 47 type sequence T description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 29) chain C residue 48 type sequence T description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 30) chain C residue 65 type sequence S description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 31) chain C residue 66 type sequence G description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 32) chain C residue 67 type sequence P description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 33) chain C residue 71 type sequence D description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 34) chain C residue 98 type sequence Q description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 35) chain D residue 150 type sequence R description BINDING SITE FOR RESIDUE PGA C 203 source : AC3 36) chain C residue 150 type sequence R description BINDING SITE FOR RESIDUE PGA D 204 source : AC4 37) chain D residue 17 type sequence V description BINDING SITE FOR RESIDUE PGA D 204 source : AC4 38) chain D residue 18 type sequence A description BINDING SITE FOR RESIDUE PGA D 204 source : AC4 39) chain D residue 23 type sequence K description BINDING SITE FOR RESIDUE PGA D 204 source : AC4 40) chain D residue 45 type sequence T description BINDING SITE FOR RESIDUE PGA D 204 source : AC4 41) chain D residue 47 type sequence T description BINDING SITE FOR RESIDUE PGA D 204 source : AC4 42) chain D residue 48 type sequence T description BINDING SITE FOR RESIDUE PGA D 204 source : AC4 43) chain D residue 65 type sequence S description BINDING SITE FOR RESIDUE PGA D 204 source : AC4 44) chain D residue 66 type sequence G description BINDING SITE FOR RESIDUE PGA D 204 source : AC4 45) chain D residue 71 type sequence D description BINDING SITE FOR RESIDUE PGA D 204 source : AC4 46) chain D residue 98 type sequence Q description BINDING SITE FOR RESIDUE PGA D 204 source : AC4 47) chain B residue 150 type sequence R description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 48) chain E residue 17 type sequence V description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 49) chain E residue 18 type sequence A description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 50) chain E residue 23 type sequence K description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 51) chain E residue 45 type sequence T description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 52) chain E residue 47 type sequence T description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 53) chain E residue 48 type sequence T description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 54) chain E residue 65 type sequence S description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 55) chain E residue 66 type sequence G description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 56) chain E residue 67 type sequence P description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 57) chain E residue 71 type sequence D description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 58) chain E residue 98 type sequence Q description BINDING SITE FOR RESIDUE PGA E 205 source : AC5 59) chain A residue 150 type sequence R description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 60) chain F residue 17 type sequence V description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 61) chain F residue 18 type sequence A description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 62) chain F residue 23 type sequence K description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 63) chain F residue 45 type sequence T description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 64) chain F residue 47 type sequence T description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 65) chain F residue 48 type sequence T description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 66) chain F residue 65 type sequence S description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 67) chain F residue 66 type sequence G description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 68) chain F residue 67 type sequence P description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 69) chain F residue 71 type sequence D description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 70) chain F residue 98 type sequence Q description BINDING SITE FOR RESIDUE PGA F 206 source : AC6 71) chain A residue 19 type catalytic sequence H description 85 source MCSA : MCSA1 72) chain A residue 66 type catalytic sequence G description 85 source MCSA : MCSA1 73) chain A residue 71 type catalytic sequence D description 85 source MCSA : MCSA1 74) chain A residue 91 type catalytic sequence D description 85 source MCSA : MCSA1 75) chain A residue 98 type catalytic sequence Q description 85 source MCSA : MCSA1 76) chain A residue 101 type catalytic sequence D description 85 source MCSA : MCSA1 77) chain A residue 107 type catalytic sequence R description 85 source MCSA : MCSA1 78) chain B residue 19 type catalytic sequence H description 85 source MCSA : MCSA2 79) chain B residue 66 type catalytic sequence G description 85 source MCSA : MCSA2 80) chain B residue 71 type catalytic sequence D description 85 source MCSA : MCSA2 81) chain B residue 91 type catalytic sequence D description 85 source MCSA : MCSA2 82) chain B residue 98 type catalytic sequence Q description 85 source MCSA : MCSA2 83) chain B residue 101 type catalytic sequence D description 85 source MCSA : MCSA2 84) chain B residue 107 type catalytic sequence R description 85 source MCSA : MCSA2 85) chain C residue 19 type catalytic sequence H description 85 source MCSA : MCSA3 86) chain C residue 66 type catalytic sequence G description 85 source MCSA : MCSA3 87) chain C residue 71 type catalytic sequence D description 85 source MCSA : MCSA3 88) chain C residue 91 type catalytic sequence D description 85 source MCSA : MCSA3 89) chain C residue 98 type catalytic sequence Q description 85 source MCSA : MCSA3 90) chain C residue 101 type catalytic sequence D description 85 source MCSA : MCSA3 91) chain C residue 107 type catalytic sequence R description 85 source MCSA : MCSA3 92) chain D residue 19 type catalytic sequence H description 85 source MCSA : MCSA4 93) chain D residue 66 type catalytic sequence G description 85 source MCSA : MCSA4 94) chain D residue 71 type catalytic sequence D description 85 source MCSA : MCSA4 95) chain D residue 91 type catalytic sequence D description 85 source MCSA : MCSA4 96) chain D residue 98 type catalytic sequence Q description 85 source MCSA : MCSA4 97) chain D residue 101 type catalytic sequence D description 85 source MCSA : MCSA4 98) chain D residue 107 type catalytic sequence R description 85 source MCSA : MCSA4 99) chain E residue 19 type catalytic sequence H description 85 source MCSA : MCSA5 100) chain E residue 66 type catalytic sequence G description 85 source MCSA : MCSA5 101) chain E residue 71 type catalytic sequence D description 85 source MCSA : MCSA5 102) chain E residue 91 type catalytic sequence D description 85 source MCSA : MCSA5 103) chain E residue 98 type catalytic sequence Q description 85 source MCSA : MCSA5 104) chain E residue 101 type catalytic sequence D description 85 source MCSA : MCSA5 105) chain E residue 107 type catalytic sequence R description 85 source MCSA : MCSA5 106) chain F residue 19 type catalytic sequence H description 85 source MCSA : MCSA6 107) chain F residue 66 type catalytic sequence G description 85 source MCSA : MCSA6 108) chain F residue 71 type catalytic sequence D description 85 source MCSA : MCSA6 109) chain F residue 91 type catalytic sequence D description 85 source MCSA : MCSA6 110) chain F residue 98 type catalytic sequence Q description 85 source MCSA : MCSA6 111) chain F residue 101 type catalytic sequence D description 85 source MCSA : MCSA6 112) chain F residue 107 type catalytic sequence R description 85 source MCSA : MCSA6 113) 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 114) 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 115) 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 116) chain D 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 117) 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 118) 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 119) 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 120) chain D 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 121) chain D 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 122) chain D 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 123) 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 124) 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 125) 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 126) 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 127) 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 128) 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 129) 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 130) 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 131) 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 132) 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 133) 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 134) 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 135) 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 136) 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 137) 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 138) 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 139) 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 140) chain D 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 141) 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 142) 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 143) chain A residue 65-73 type prosite sequence SGPMGGDQQ description METHYLGLYOXAL_SYNTH Methylglyoxal synthase active site. SGPMGGDqQ source prosite : PS01335 144) 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 145) 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 146) 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 147) chain D 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 148) 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 149) 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

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