eF-site ID 1bxk-B PDB Code 1bxk Chain B 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 B:  MRKILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGN LMSLAPVAQSERFAFEKVDICDRAELARVFTEHQPDCVMH LAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNALT EDKKSAFRFHHISTDEVYGDLHSTDDFFTETTPYAPSSPY SASKASSDHLVRAWLRTYGLPTLITNCSNNYGPYHFPEKL IPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALYCVA TTGKVGETYNIGGHNERKNLDVVETICELLEELAPNKPHG VAHYRDLITFVALRYAIDASKIARELGCVPQETFESGMRK TVQWYLANESWWKQVQDGSYQGER Description Functional site 1) chain B residue 408 type sequence G description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 2) chain B residue 410 type sequence A description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 3) chain B residue 411 type sequence G description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 4) chain B residue 412 type sequence F description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 5) chain B residue 413 type sequence I description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 6) chain B residue 433 type sequence D description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 7) chain B residue 434 type sequence K description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 8) chain B residue 435 type sequence L description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 9) chain B residue 436 type sequence T description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 10) chain B residue 438 type sequence A description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 11) chain B residue 439 type sequence G description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 12) chain B residue 458 type sequence V description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 13) chain B residue 459 type sequence D description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 14) chain B residue 460 type sequence I description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 15) chain B residue 481 type sequence L description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 16) chain B residue 483 type sequence A description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 17) chain B residue 500 type sequence T description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 18) chain B residue 532 type sequence I description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 19) chain B residue 533 type sequence S description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 20) chain B residue 534 type sequence T description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 21) chain B residue 560 type sequence Y description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 22) chain B residue 564 type sequence K description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 23) chain B residue 587 type sequence C description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 24) chain B residue 588 type sequence S description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 25) chain B residue 590 type sequence N description BINDING SITE FOR RESIDUE NAD B 780 source : AC2 26) 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 27) chain B residue 534 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 28) chain B residue 589 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 29) chain B residue 599 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 30) chain B residue 615 type BINDING sequence P description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 31) chain B residue 624 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 32) chain B residue 659 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 33) chain B residue 485 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P26391 source Swiss-Prot : SWS_FT_FI5 34) chain B residue 534 type catalytic sequence T description 228 source MCSA : MCSA2 35) chain B residue 535 type catalytic sequence D description 228 source MCSA : MCSA2 36) chain B residue 536 type catalytic sequence E description 228 source MCSA : MCSA2 37) chain B residue 560 type catalytic sequence Y description 228 source MCSA : MCSA2 38) chain B residue 564 type catalytic sequence K description 228 source MCSA : MCSA2 39) 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 40) 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 41) chain B residue 500 type BINDING sequence T description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 42) chain B residue 560 type BINDING sequence Y description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 43) chain B residue 590 type BINDING sequence N description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 44) chain B residue 412 type BINDING sequence F description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 45) chain B residue 433 type BINDING sequence D description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 46) chain B residue 459 type BINDING sequence D description BINDING => ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI3 47) chain B residue 481 type BINDING sequence L description BINDING => ECO:0000305|Ref.8, ECO:0007744|PDB:1BXK source Swiss-Prot : SWS_FT_FI4

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