eF-site ID 1bxk-A PDB Code 1bxk Chain A click to enlarge Title DTDP-GLUCOSE 4,6-DEHYDRATASE FROM E. COLI Classification LYASE Compound PROTEIN (DTDP-GLUCOSE 4,6-DEHYDRATASE) Source Escherichia coli (strain K12) (RFFG_ECOLI) Sequence A:  MRKILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGN LMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVMH LAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNALT EDKKSAFRFHHISTDEVYGDLHSTDDFFTETTPYAPSSPY SASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKL IPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALYCVA TTGKVGETYNIGGHNERKNLDVVETICELLEELAPNKPHG VAHYRDLITFRYAIDASKIARELGCVPQETFESGMRKTVQ WYLANESWWKQVQDGSYQGER Description Functional site 1) chain A residue 8 type sequence G description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 2) chain A residue 10 type sequence A description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 3) chain A residue 11 type sequence G description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 4) chain A residue 12 type sequence F description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 5) chain A residue 13 type sequence I description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 6) chain A residue 33 type sequence D description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 7) chain A residue 34 type sequence K description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 8) chain A residue 35 type sequence L description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 9) chain A residue 36 type sequence T description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 10) chain A residue 38 type sequence A description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 11) chain A residue 39 type sequence G description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 12) chain A residue 58 type sequence V description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 13) chain A residue 59 type sequence D description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 14) chain A residue 60 type sequence I description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 15) chain A residue 81 type sequence L description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 16) chain A residue 83 type sequence A description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 17) chain A residue 100 type sequence T description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 18) chain A residue 132 type sequence I description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 19) chain A residue 133 type sequence S description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 20) chain A residue 134 type sequence T description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 21) chain A residue 160 type sequence Y description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 22) chain A residue 164 type sequence K description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 23) chain A residue 187 type sequence C description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 24) chain A residue 188 type sequence S description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 25) chain A residue 189 type sequence N description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 26) chain A residue 190 type sequence N description BINDING SITE FOR RESIDUE NAD A 380 source : AC1 27) chain A residue 135 type ACT_SITE sequence D description Proton donor => ECO:0000269|PubMed:11380254, ECO:0000269|PubMed:11601973 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 85 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 29) chain A residue 134 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 30) chain A residue 189 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 31) chain A residue 199 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 32) chain A residue 215 type BINDING sequence P description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 33) chain A residue 224 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 34) chain A residue 259 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 35) chain A residue 134 type catalytic sequence T description 228 source MCSA : MCSA1 36) chain A residue 135 type catalytic sequence D description 228 source MCSA : MCSA1 37) chain A residue 136 type catalytic sequence E description 228 source MCSA : MCSA1 38) chain A residue 160 type catalytic sequence Y description 228 source MCSA : MCSA1 39) chain A residue 164 type catalytic sequence K description 228 source MCSA : MCSA1 40) chain A residue 136 type ACT_SITE sequence E description Proton acceptor => ECO:0000269|PubMed:11380254, ECO:0000269|PubMed:11601973 source Swiss-Prot : SWS_FT_FI2 41) chain A residue 160 type ACT_SITE sequence Y description Proton acceptor => ECO:0000269|PubMed:11380254, ECO:0000269|PubMed:11601973 source Swiss-Prot : SWS_FT_FI2 42) chain A residue 12 type BINDING sequence F description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 43) chain A residue 33 type BINDING sequence D description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 44) chain A residue 59 type BINDING sequence D description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 45) chain A residue 100 type BINDING sequence T description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 46) chain A residue 160 type BINDING sequence Y description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 47) chain A residue 190 type BINDING sequence N description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 48) chain A residue 81 type BINDING sequence L description BINDING => ECO:0000305|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI4

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