eF-site ID 1bxk-AB PDB Code 1bxk Chain A, B click to enlarge Title DTDP-GLUCOSE 4,6-DEHYDRATASE FROM E. COLI Classification LYASE Compound PROTEIN (DTDP-GLUCOSE 4,6-DEHYDRATASE) Source null (RFFG_ECOLI) Sequence A:  MRKILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGN LMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVMH LAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNALT EDKKSAFRFHHISTDEVYGDLHSTDDFFTETTPYAPSSPY SASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKL IPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALYCVA TTGKVGETYNIGGHNERKNLDVVETICELLEELAPNKPHG VAHYRDLITFRYAIDASKIARELGCVPQETFESGMRKTVQ WYLANESWWKQVQDGSYQGER B:  MRKILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGN LMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVMH LAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNALT EDKKSAFRFHHISTDEVYGDLHSTDDFFTETTPYAPSSPY SASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKL IPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALYCVA TTGKVGETYNIGGHNERKNLDVVETICELLEELAPNKPHG VAHYRDLITFVALRYAIDASKIARELGCVPQETFESGMRK TVQWYLANESWWKQVQDGSYQGER 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 B residue 408 type sequence G description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 28) chain B residue 410 type sequence A description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 29) chain B residue 411 type sequence G description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 30) chain B residue 412 type sequence F description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 31) chain B residue 413 type sequence I description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 32) chain B residue 433 type sequence D description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 33) chain B residue 434 type sequence K description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 34) chain B residue 435 type sequence L description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 35) chain B residue 436 type sequence T description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 36) chain B residue 438 type sequence A description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 37) chain B residue 439 type sequence G description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 38) chain B residue 458 type sequence V description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 39) chain B residue 459 type sequence D description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 40) chain B residue 460 type sequence I description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 41) chain B residue 481 type sequence L description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 42) chain B residue 483 type sequence A description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 43) chain B residue 500 type sequence T description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 44) chain B residue 532 type sequence I description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 45) chain B residue 533 type sequence S description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 46) chain B residue 534 type sequence T description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 47) chain B residue 560 type sequence Y description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 48) chain B residue 564 type sequence K description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 49) chain B residue 587 type sequence C description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 50) chain B residue 588 type sequence S description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 51) chain B residue 590 type sequence N description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 52) chain A residue 134 type catalytic sequence T description 228 source MCSA : MCSA1 53) chain A residue 135 type catalytic sequence D description 228 source MCSA : MCSA1 54) chain A residue 136 type catalytic sequence E description 228 source MCSA : MCSA1 55) chain A residue 160 type catalytic sequence Y description 228 source MCSA : MCSA1 56) chain A residue 164 type catalytic sequence K description 228 source MCSA : MCSA1 57) chain B residue 534 type catalytic sequence T description 228 source MCSA : MCSA2 58) chain B residue 535 type catalytic sequence D description 228 source MCSA : MCSA2 59) chain B residue 536 type catalytic sequence E description 228 source MCSA : MCSA2 60) chain B residue 560 type catalytic sequence Y description 228 source MCSA : MCSA2 61) chain B residue 564 type catalytic sequence K description 228 source MCSA : MCSA2 62) 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 63) chain B residue 535 type ACT_SITE sequence D description Proton donor => ECO:0000269|PubMed:11380254, ECO:0000269|PubMed:11601973 source Swiss-Prot : SWS_FT_FI1 64) 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 65) chain B residue 536 type ACT_SITE sequence E description Proton acceptor => ECO:0000269|PubMed:11380254, ECO:0000269|PubMed:11601973 source Swiss-Prot : SWS_FT_FI2 66) chain B residue 560 type ACT_SITE sequence Y description Proton acceptor => ECO:0000269|PubMed:11380254, ECO:0000269|PubMed:11601973 source Swiss-Prot : SWS_FT_FI2 67) 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 68) chain A residue 12 type BINDING sequence F description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 69) chain B residue 500 type BINDING sequence T description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 70) chain B residue 560 type BINDING sequence Y description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 71) chain B residue 590 type BINDING sequence N description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 72) chain A residue 59 type BINDING sequence D description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 73) chain A residue 100 type BINDING sequence T description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 74) chain A residue 160 type BINDING sequence Y description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 75) chain A residue 190 type BINDING sequence N description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 76) chain B residue 412 type BINDING sequence F description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 77) chain B residue 433 type BINDING sequence D description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 78) chain B residue 459 type BINDING sequence D description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 79) chain A residue 33 type BINDING sequence D description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 80) chain A residue 81 type BINDING sequence L description BINDING => ECO:0000305|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI4 81) chain B residue 481 type BINDING sequence L description BINDING => ECO:0000305|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI4 82) chain A residue 85 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 83) chain A residue 134 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 84) chain B residue 534 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 85) chain B residue 589 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 86) chain B residue 599 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 87) chain B residue 615 type BINDING sequence P description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 88) chain B residue 624 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 89) chain B residue 659 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 90) chain A residue 189 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 91) chain A residue 199 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 92) chain A residue 215 type BINDING sequence P description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 93) chain A residue 224 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 94) chain A residue 259 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 95) chain B residue 485 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5

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