eF-site ID 1hzj-A PDB Code 1hzj Chain A click to enlarge Title HUMAN UDP-GALACTOSE 4-EPIMERASE: ACCOMMODATION OF UDP-N-ACETYLGLUCOSAMINE WITHIN THE ACTIVE SITE Classification ISOMERASE Compound UDP-GALACTOSE 4-EPIMERASE Source null (GALE_HUMAN) Sequence A:  AEKVLVTGGAGYIGSHTVLELLEAGYLPVVIDNFHNAFRG GGSLPESLRRVQELTGRSVEFEEMDILDQGALQRLFKKYS FMAVIHFAGLKAVGESVQKPLDYYRVNLTGTIQLLEIMKA HGVKNLVFSSSATVYGNPQYLPLDEAHPTGGCTNPYGKSK FFIEEMIRDLCQADKTWNVVLLRYFNPTGAHASGCIGEDP QGIPNNLMPYVSQVAIGRREALNVFGNDYDTEDGTGVRDY IHVVDLAKGHIAALRKLKEQCGCRIYNLGTGTGYSVLQMV QAMEKASGKKIPYKVVARREGDVAACYANPSLAQEELGWT AALGLDRMCEDLWRWQKQNPSGFGT Description Functional site 1) chain A residue 100 type sequence K description BINDING SITE FOR RESIDUE CL A 950 source : AC1 2) chain A residue 101 type sequence P description BINDING SITE FOR RESIDUE CL A 950 source : AC1 3) chain A residue 102 type sequence L description BINDING SITE FOR RESIDUE CL A 950 source : AC1 4) chain A residue 4 type sequence K description BINDING SITE FOR RESIDUE CL A 952 source : AC3 5) chain A residue 80 type sequence Y description BINDING SITE FOR RESIDUE CL A 952 source : AC3 6) chain A residue 81 type sequence S description BINDING SITE FOR RESIDUE CL A 952 source : AC3 7) chain A residue 9 type sequence G description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 8) chain A residue 12 type sequence G description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 9) chain A residue 13 type sequence Y description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 10) chain A residue 14 type sequence I description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 11) chain A residue 33 type sequence D description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 12) chain A residue 34 type sequence N description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 13) chain A residue 35 type sequence F description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 14) chain A residue 36 type sequence H description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 15) chain A residue 37 type sequence N description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 16) chain A residue 65 type sequence M description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 17) chain A residue 66 type sequence D description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 18) chain A residue 67 type sequence I description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 19) chain A residue 88 type sequence F description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 20) chain A residue 89 type sequence A description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 21) chain A residue 90 type sequence G description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 22) chain A residue 92 type sequence K description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 23) chain A residue 130 type sequence S description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 24) chain A residue 131 type sequence S description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 25) chain A residue 132 type sequence S description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 26) chain A residue 157 type sequence Y description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 27) chain A residue 161 type sequence K description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 28) chain A residue 185 type sequence Y description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 29) chain A residue 188 type sequence P description BINDING SITE FOR RESIDUE NAD A 400 source : AC5 30) chain A residue 94 type sequence V description BINDING SITE FOR RESIDUE UD1 A 401 source : AC6 31) chain A residue 132 type sequence S description BINDING SITE FOR RESIDUE UD1 A 401 source : AC6 32) chain A residue 134 type sequence T description BINDING SITE FOR RESIDUE UD1 A 401 source : AC6 33) chain A residue 187 type sequence N description BINDING SITE FOR RESIDUE UD1 A 401 source : AC6 34) chain A residue 206 type sequence N description BINDING SITE FOR RESIDUE UD1 A 401 source : AC6 35) chain A residue 207 type sequence N description BINDING SITE FOR RESIDUE UD1 A 401 source : AC6 36) chain A residue 208 type sequence L description BINDING SITE FOR RESIDUE UD1 A 401 source : AC6 37) chain A residue 223 type sequence L description BINDING SITE FOR RESIDUE UD1 A 401 source : AC6 38) chain A residue 224 type sequence N description BINDING SITE FOR RESIDUE UD1 A 401 source : AC6 39) chain A residue 225 type sequence V description BINDING SITE FOR RESIDUE UD1 A 401 source : AC6 40) chain A residue 226 type sequence F description BINDING SITE FOR RESIDUE UD1 A 401 source : AC6 41) chain A residue 237 type sequence G description BINDING SITE FOR RESIDUE UD1 A 401 source : AC6 42) chain A residue 239 type sequence R description BINDING SITE FOR RESIDUE UD1 A 401 source : AC6 43) chain A residue 241 type sequence Y description BINDING SITE FOR RESIDUE UD1 A 401 source : AC6 44) chain A residue 277 type sequence V description BINDING SITE FOR RESIDUE UD1 A 401 source : AC6 45) chain A residue 300 type sequence R description BINDING SITE FOR RESIDUE UD1 A 401 source : AC6 46) chain A residue 303 type sequence D description BINDING SITE FOR RESIDUE UD1 A 401 source : AC6 47) chain A residue 157 type ACT_SITE sequence Y description Proton acceptor => ECO:0000269|PubMed:10801319, ECO:0000269|PubMed:11279032, ECO:0000269|PubMed:11279193, ECO:0000303|PubMed:15175331 source Swiss-Prot : SWS_FT_FI1 48) chain A residue 33 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10801319, ECO:0000269|PubMed:11279032, ECO:0000269|PubMed:11279193 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 66 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10801319, ECO:0000269|PubMed:11279032, ECO:0000269|PubMed:11279193 source Swiss-Prot : SWS_FT_FI2 50) chain A residue 88 type BINDING sequence F description BINDING => ECO:0000269|PubMed:10801319, ECO:0000269|PubMed:11279032, ECO:0000269|PubMed:11279193 source Swiss-Prot : SWS_FT_FI2 51) chain A residue 92 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10801319, ECO:0000269|PubMed:11279032, ECO:0000269|PubMed:11279193 source Swiss-Prot : SWS_FT_FI2 52) chain A residue 161 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10801319, ECO:0000269|PubMed:11279032, ECO:0000269|PubMed:11279193 source Swiss-Prot : SWS_FT_FI2 53) chain A residue 206 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10801319, ECO:0000269|PubMed:11279032, ECO:0000269|PubMed:11279193 source Swiss-Prot : SWS_FT_FI2 54) chain A residue 224 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10801319, ECO:0000269|PubMed:11279032, ECO:0000269|PubMed:11279193 source Swiss-Prot : SWS_FT_FI2 55) chain A residue 239 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10801319, ECO:0000269|PubMed:11279032, ECO:0000269|PubMed:11279193 source Swiss-Prot : SWS_FT_FI2 56) chain A residue 12 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10801319, ECO:0000269|PubMed:11279032, ECO:0000269|PubMed:11279193 source Swiss-Prot : SWS_FT_FI2 57) chain A residue 132 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10801319, ECO:0000269|PubMed:11279032, ECO:0000269|PubMed:11279193, ECO:0000303|PubMed:15175331 source Swiss-Prot : SWS_FT_FI3 58) chain A residue 185 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10801319 source Swiss-Prot : SWS_FT_FI4 59) chain A residue 300 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11279032, ECO:0000269|PubMed:11279193 source Swiss-Prot : SWS_FT_FI5

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