eF-site ID 1eq2-A PDB Code 1eq2 Chain A click to enlarge Title THE CRYSTAL STRUCTURE OF ADP-L-GLYCERO-D-MANNOHEPTOSE 6-EPIMERASE Classification ISOMERASE Compound ADP-L-GLYCERO-D-MANNOHEPTOSE 6-EPIMERASE Source Escherichia coli (strain K12) (HLDD_ECOLI) Sequence A:  MIIVTGGAGFIGSNIVKALNDKGITDILVVDNLKDGTKFV NLVDLNIADYMDKEDFLIQIMAGEEFGDVEAIFHEGAXSS TTEWDGKYMMDNNYQYSKELLHYCLEREIPFLYASSAATY GGRTSDFIESREYEKPLNVYGYSKFLFDEYVRQILPEANS QIVGFRYFNVYGPREGHKGSMASVAFHLNTQLNNKRDFVY VGDVADVNLWFLENGVSGIFNLGTGRAESFQAVADATYQA FTQADLTNLRAAGYDKPFKTVAEGVTEYMAWLN Description Functional site 1) chain A residue 6 type sequence G description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 2) chain A residue 9 type sequence G description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 3) chain A residue 10 type sequence F description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 4) chain A residue 11 type sequence I description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 5) chain A residue 31 type sequence D description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 6) chain A residue 32 type sequence N description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 7) chain A residue 38 type sequence K description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 8) chain A residue 53 type sequence K description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 9) chain A residue 75 type sequence E description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 10) chain A residue 76 type sequence G description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 11) chain A residue 77 type sequence A description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 12) chain A residue 79 type sequence S description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 13) chain A residue 92 type sequence N description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 14) chain A residue 96 type sequence Y description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 15) chain A residue 114 type sequence A description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 16) chain A residue 115 type sequence S description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 17) chain A residue 116 type sequence S description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 18) chain A residue 140 type sequence Y description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 19) chain A residue 144 type sequence K description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 20) chain A residue 167 type sequence Y description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 21) chain A residue 168 type sequence F description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 22) chain A residue 170 type sequence V description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 23) chain A residue 177 type sequence H description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 24) chain A residue 178 type sequence K description BINDING SITE FOR RESIDUE NAP A 2400 source : AC1 25) chain A residue 81 type sequence T description BINDING SITE FOR RESIDUE ADQ A 2500 source : AC2 26) chain A residue 169 type sequence N description BINDING SITE FOR RESIDUE ADQ A 2500 source : AC2 27) chain A residue 180 type sequence S description BINDING SITE FOR RESIDUE ADQ A 2500 source : AC2 28) chain A residue 182 type sequence A description BINDING SITE FOR RESIDUE ADQ A 2500 source : AC2 29) chain A residue 187 type sequence H description BINDING SITE FOR RESIDUE ADQ A 2500 source : AC2 30) chain A residue 209 type sequence R description BINDING SITE FOR RESIDUE ADQ A 2500 source : AC2 31) chain A residue 243 type sequence F description BINDING SITE FOR RESIDUE ADQ A 2500 source : AC2 32) chain A residue 116 type catalytic sequence S description 557 source MCSA : MCSA1 33) chain A residue 140 type catalytic sequence Y description 557 source MCSA : MCSA1 34) chain A residue 178 type catalytic sequence K description 557 source MCSA : MCSA1 35) chain A residue 140 type ACT_SITE sequence Y description Proton acceptor => ECO:0000269|PubMed:17316025 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 178 type ACT_SITE sequence K description Proton acceptor => ECO:0000269|PubMed:17316025 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 10 type BINDING sequence F description BINDING => ECO:0000269|PubMed:10896473 source Swiss-Prot : SWS_FT_FI2 38) chain A residue 178 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10896473 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 180 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10896473 source Swiss-Prot : SWS_FT_FI2 40) chain A residue 187 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10896473 source Swiss-Prot : SWS_FT_FI2 41) chain A residue 209 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10896473 source Swiss-Prot : SWS_FT_FI2 42) chain A residue 272 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10896473 source Swiss-Prot : SWS_FT_FI2 43) chain A residue 31 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10896473 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 38 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10896473 source Swiss-Prot : SWS_FT_FI2 45) chain A residue 53 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10896473 source Swiss-Prot : SWS_FT_FI2 46) chain A residue 75 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10896473 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 92 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10896473 source Swiss-Prot : SWS_FT_FI2 48) chain A residue 144 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10896473 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 169 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10896473 source Swiss-Prot : SWS_FT_FI2 50) chain A residue 170 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10896473 source Swiss-Prot : SWS_FT_FI2

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