eF-site ID 3cmc-Q PDB Code 3cmc Chain Q click to enlarge Title Thioacylenzyme intermediate of Bacillus stearothermophilus phosphorylating GAPDH Classification OXIDOREDUCTASE Compound Glyceraldehyde-3-phosphate dehydrogenase Source Geobacillus stearothermophilus (Bacillus stearothermophilus) (G3P_BACST) Sequence Q:  AVKVGINGFGRIGRNVFRAALKNPDIEVVAVNDLTDANTL AHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERDPE NLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISA PAKNEDITIVMGVNQDKYDPKAHHVISNASCTTNCLAPFA KVLHEQFGIVRGMMTTVHSYTNDQRILDLPHKDLRRARAA AESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNVSV VDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLV SRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNETGYSH RVVDLAAYIASKGL Description (1)  Glyceraldehyde-3-phosphate dehydrogenase (E.C.1.2.1.12) Functional site 1) chain Q residue 121 type sequence P description BINDING SITE FOR RESIDUE SO4 Q 401 source : AC3 2) chain Q residue 148 type sequence S description BINDING SITE FOR RESIDUE SO4 Q 401 source : AC3 3) chain Q residue 207 type sequence T description BINDING SITE FOR RESIDUE SO4 Q 401 source : AC3 4) chain Q residue 208 type sequence T description BINDING SITE FOR RESIDUE SO4 Q 401 source : AC3 5) chain Q residue 209 type sequence G description BINDING SITE FOR RESIDUE SO4 Q 401 source : AC3 6) chain Q residue 210 type sequence A description BINDING SITE FOR RESIDUE SO4 Q 401 source : AC3 7) chain Q residue 179 type sequence T description BINDING SITE FOR RESIDUE SO4 Q 402 source : AC7 8) chain Q residue 181 type sequence D description BINDING SITE FOR RESIDUE SO4 Q 402 source : AC7 9) chain Q residue 195 type sequence R description BINDING SITE FOR RESIDUE SO4 Q 402 source : AC7 10) chain Q residue 231 type sequence R description BINDING SITE FOR RESIDUE SO4 Q 402 source : AC7 11) chain Q residue 303 type sequence K description BINDING SITE FOR RESIDUE SO4 R 403 source : BC2 12) chain Q residue 183 type sequence R description BINDING SITE FOR RESIDUE SO4 Q 403 source : BC3 13) chain Q residue 188 type sequence P description BINDING SITE FOR RESIDUE SO4 Q 403 source : BC3 14) chain Q residue 190 type sequence H description BINDING SITE FOR RESIDUE SO4 Q 403 source : BC3 15) chain Q residue 191 type sequence K description BINDING SITE FOR RESIDUE SO4 Q 403 source : BC3 16) chain Q residue 148 type sequence S description BINDING SITE FOR RESIDUE G3H Q 400 source : CC3 17) chain Q residue 149 type sequence C description BINDING SITE FOR RESIDUE G3H Q 400 source : CC3 18) chain Q residue 150 type sequence T description BINDING SITE FOR RESIDUE G3H Q 400 source : CC3 19) chain Q residue 176 type sequence H description BINDING SITE FOR RESIDUE G3H Q 400 source : CC3 20) chain Q residue 179 type sequence T description BINDING SITE FOR RESIDUE G3H Q 400 source : CC3 21) chain Q residue 208 type sequence T description BINDING SITE FOR RESIDUE G3H Q 400 source : CC3 22) chain Q residue 209 type sequence G description BINDING SITE FOR RESIDUE G3H Q 400 source : CC3 23) chain Q residue 231 type sequence R description BINDING SITE FOR RESIDUE G3H Q 400 source : CC3 24) chain Q residue 7 type sequence G description BINDING SITE FOR RESIDUE NAD Q 404 source : CC7 25) chain Q residue 9 type sequence G description BINDING SITE FOR RESIDUE NAD Q 404 source : CC7 26) chain Q residue 10 type sequence R description BINDING SITE FOR RESIDUE NAD Q 404 source : CC7 27) chain Q residue 11 type sequence I description BINDING SITE FOR RESIDUE NAD Q 404 source : CC7 28) chain Q residue 31 type sequence N description BINDING SITE FOR RESIDUE NAD Q 404 source : CC7 29) chain Q residue 32 type sequence D description BINDING SITE FOR RESIDUE NAD Q 404 source : CC7 30) chain Q residue 33 type sequence L description BINDING SITE FOR RESIDUE NAD Q 404 source : CC7 31) chain Q residue 77 type sequence R description BINDING SITE FOR RESIDUE NAD Q 404 source : CC7 32) chain Q residue 95 type sequence S description BINDING SITE FOR RESIDUE NAD Q 404 source : CC7 33) chain Q residue 96 type sequence T description BINDING SITE FOR RESIDUE NAD Q 404 source : CC7 34) chain Q residue 97 type sequence G description BINDING SITE FOR RESIDUE NAD Q 404 source : CC7 35) chain Q residue 98 type sequence R description BINDING SITE FOR RESIDUE NAD Q 404 source : CC7 36) chain Q residue 99 type sequence F description BINDING SITE FOR RESIDUE NAD Q 404 source : CC7 37) chain Q residue 119 type sequence S description BINDING SITE FOR RESIDUE NAD Q 404 source : CC7 38) chain Q residue 120 type sequence A description BINDING SITE FOR RESIDUE NAD Q 404 source : CC7 39) chain Q residue 180 type sequence N description BINDING SITE FOR RESIDUE NAD Q 404 source : CC7 40) chain Q residue 313 type sequence N description BINDING SITE FOR RESIDUE NAD Q 404 source : CC7 41) chain Q residue 317 type sequence Y description BINDING SITE FOR RESIDUE NAD Q 404 source : CC7 42) chain Q residue 134 type sequence Q description BINDING SITE FOR RESIDUE EDO Q 405 source : CC9 43) chain Q residue 135 type sequence D description BINDING SITE FOR RESIDUE EDO Q 405 source : CC9 44) chain Q residue 159 type sequence K description BINDING SITE FOR RESIDUE EDO Q 405 source : CC9 45) chain Q residue 169 type sequence R description BINDING SITE FOR RESIDUE GOL R 409 source : DC1 46) chain Q residue 14 type sequence N description BINDING SITE FOR RESIDUE GOL Q 406 source : DC7 47) chain Q residue 17 type sequence R description BINDING SITE FOR RESIDUE GOL Q 406 source : DC7 48) chain Q residue 50 type sequence H description BINDING SITE FOR RESIDUE GOL Q 406 source : DC7 49) chain Q residue 315 type sequence T description BINDING SITE FOR RESIDUE GOL Q 406 source : DC7 50) chain Q residue 149 type ACT_SITE sequence C description Nucleophile => ECO:0000269|PubMed:18480053, ECO:0000305|PubMed:12569100 source Swiss-Prot : SWS_FT_FI1 51) chain Q residue 10 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858 source Swiss-Prot : SWS_FT_FI2 52) chain Q residue 32 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858 source Swiss-Prot : SWS_FT_FI2 53) chain Q residue 77 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858 source Swiss-Prot : SWS_FT_FI2 54) chain Q residue 119 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858 source Swiss-Prot : SWS_FT_FI2 55) chain Q residue 180 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858 source Swiss-Prot : SWS_FT_FI2 56) chain Q residue 313 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858 source Swiss-Prot : SWS_FT_FI2 57) chain Q residue 148 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3210237, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858 source Swiss-Prot : SWS_FT_FI3 58) chain Q residue 179 type BINDING sequence T description BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3210237, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858 source Swiss-Prot : SWS_FT_FI3 59) chain Q residue 231 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3210237, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858 source Swiss-Prot : SWS_FT_FI3 60) chain Q residue 195 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:9175858 source Swiss-Prot : SWS_FT_FI4 61) chain Q residue 208 type BINDING sequence T description BINDING => ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3210237, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858 source Swiss-Prot : SWS_FT_FI5 62) chain Q residue 176 type SITE sequence H description Activates thiol group during catalysis => ECO:0000250|UniProtKB:Q6GIL8 source Swiss-Prot : SWS_FT_FI6

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