eF-site ID 1tpb-12 PDB Code 1tpb Chain 1, 2 click to enlarge Title OFFSET OF A CATALYTIC LESION BY A BOUND WATER SOLUBLE Classification ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) Compound TRIOSEPHOSPHATE ISOMERASE Source null (TPIS_CHICK) Sequence 1:  RKFFVGGNWKMNGDKKSLGELIHTLNGAKLSADTEVVCGA PSIYLDFARQKLDAKIGVAAQNCYKVPKGAFTGEISPAMI KDIGAAWVILGHSERRHVFGESDELIGQKVAHALAEGLGV IACIGEKLDEREAGITEKVVFEQTKAIADNVKDWSKVVLA YDPVWAIGTGKTATPQQAQEVHEKLRGWLKTHVSDAVAQS TRIIYGGSVTGGNCKELASQHDVDGFLVGGASLKPEFVDI INAKH 2:  RKFFVGGNWKMNGDKKSLGELIHTLNGAKLSADTEVVCGA PSIYLDFARQKLDAKIGVAAQNCYKVPKGAFTGEISPAMI KDIGAAWVILGHSERRHVFGESDELIGQKVAHALAEGLGV IACIGEKLDEREAGITEKVVFEQTKAIADNVKDWSKVVLA YDPVWAIGTGKTATPQQAQEVHEKLRGWLKTHVSDAVAQS TRIIYGGSVTGGNCKELASQHDVDGFLVGGASLKPEFVDI INAKH Description Functional site 1) chain 1 residue 165 type sequence D description source : AC1 2) chain 1 residue 95 type sequence H description source : AC1 3) chain 1 residue 96 type sequence S description source : AC1 4) chain 1 residue 13 type sequence K description source : AC1 5) chain 2 residue 165 type sequence D description source : AC2 6) chain 2 residue 95 type sequence H description source : AC2 7) chain 2 residue 96 type sequence S description source : AC2 8) chain 2 residue 13 type sequence K description source : AC2 9) chain 1 residue 13 type sequence K description BINDING SITE FOR RESIDUE PGH 1 250 source : AC3 10) chain 1 residue 95 type sequence H description BINDING SITE FOR RESIDUE PGH 1 250 source : AC3 11) chain 1 residue 165 type sequence D description BINDING SITE FOR RESIDUE PGH 1 250 source : AC3 12) chain 1 residue 169 type sequence A description BINDING SITE FOR RESIDUE PGH 1 250 source : AC3 13) chain 1 residue 170 type sequence I description BINDING SITE FOR RESIDUE PGH 1 250 source : AC3 14) chain 1 residue 171 type sequence G description BINDING SITE FOR RESIDUE PGH 1 250 source : AC3 15) chain 1 residue 211 type sequence S description BINDING SITE FOR RESIDUE PGH 1 250 source : AC3 16) chain 1 residue 230 type sequence L description BINDING SITE FOR RESIDUE PGH 1 250 source : AC3 17) chain 1 residue 232 type sequence G description BINDING SITE FOR RESIDUE PGH 1 250 source : AC3 18) chain 1 residue 233 type sequence G description BINDING SITE FOR RESIDUE PGH 1 250 source : AC3 19) chain 2 residue 13 type sequence K description BINDING SITE FOR RESIDUE PGH 2 250 source : AC4 20) chain 2 residue 95 type sequence H description BINDING SITE FOR RESIDUE PGH 2 250 source : AC4 21) chain 2 residue 165 type sequence D description BINDING SITE FOR RESIDUE PGH 2 250 source : AC4 22) chain 2 residue 169 type sequence A description BINDING SITE FOR RESIDUE PGH 2 250 source : AC4 23) chain 2 residue 170 type sequence I description BINDING SITE FOR RESIDUE PGH 2 250 source : AC4 24) chain 2 residue 171 type sequence G description BINDING SITE FOR RESIDUE PGH 2 250 source : AC4 25) chain 2 residue 210 type sequence G description BINDING SITE FOR RESIDUE PGH 2 250 source : AC4 26) chain 2 residue 211 type sequence S description BINDING SITE FOR RESIDUE PGH 2 250 source : AC4 27) chain 2 residue 230 type sequence L description BINDING SITE FOR RESIDUE PGH 2 250 source : AC4 28) chain 2 residue 232 type sequence G description BINDING SITE FOR RESIDUE PGH 2 250 source : AC4 29) chain 2 residue 233 type sequence G description BINDING SITE FOR RESIDUE PGH 2 250 source : AC4 30) chain 1 residue 96 type ACT_SITE sequence S description Electrophile => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH source Swiss-Prot : SWS_FT_FI1 31) chain 2 residue 96 type ACT_SITE sequence S description Electrophile => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH source Swiss-Prot : SWS_FT_FI1 32) chain 1 residue 166 type ACT_SITE sequence P description Proton acceptor => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH source Swiss-Prot : SWS_FT_FI2 33) chain 2 residue 166 type ACT_SITE sequence P description Proton acceptor => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH source Swiss-Prot : SWS_FT_FI2 34) chain 1 residue 12 type BINDING sequence W description BINDING => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH source Swiss-Prot : SWS_FT_FI3 35) chain 1 residue 14 type BINDING sequence M description BINDING => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH source Swiss-Prot : SWS_FT_FI3 36) chain 2 residue 12 type BINDING sequence W description BINDING => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH source Swiss-Prot : SWS_FT_FI3 37) chain 2 residue 14 type BINDING sequence M description BINDING => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH source Swiss-Prot : SWS_FT_FI3 38) chain 1 residue 12 type catalytic sequence W description 324 source MCSA : MCSA1 39) chain 1 residue 14 type catalytic sequence M description 324 source MCSA : MCSA1 40) chain 1 residue 96 type catalytic sequence S description 324 source MCSA : MCSA1 41) chain 1 residue 98 type catalytic sequence R description 324 source MCSA : MCSA1 42) chain 1 residue 166 type catalytic sequence P description 324 source MCSA : MCSA1 43) chain 1 residue 172 type catalytic sequence T description 324 source MCSA : MCSA1 44) chain 1 residue 212 type catalytic sequence V description 324 source MCSA : MCSA1 45) chain 2 residue 12 type catalytic sequence W description 324 source MCSA : MCSA2 46) chain 2 residue 14 type catalytic sequence M description 324 source MCSA : MCSA2 47) chain 2 residue 96 type catalytic sequence S description 324 source MCSA : MCSA2 48) chain 2 residue 98 type catalytic sequence R description 324 source MCSA : MCSA2 49) chain 2 residue 166 type catalytic sequence P description 324 source MCSA : MCSA2 50) chain 2 residue 172 type catalytic sequence T description 324 source MCSA : MCSA2 51) chain 2 residue 212 type catalytic sequence V description 324 source MCSA : MCSA2

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