eF-site ID 4pxq-AB PDB Code 4pxq Chain A, B click to enlarge Title Crystal structure of D-glucuronyl C5-epimerase in complex with heparin hexasaccharide Classification ISOMERASE Compound D-glucuronyl C5 epimerase B Source (Q6TS32_DANRE) Sequence A:  GVRYEEIDCLINDDATIKGRREGSEVYMPFSWMEKYFEVY GKVVQYDGYDRFEFSHSYSKVYAQREQYHPNGVFMSFEGY NVEVRDRVKCISGVEGVPLSTQWGPQGYFYAIQIAQYGLS HYSKNLTERPPHVEVYDTAEERDSRSSAWTVPKGCSLTRV YDKTRATSVREFSAPENSEGVSLPLGNTKDFIISFDLKFT SNGSVSVILETTEKGPPFVIHYVTTTQLILLKDRDITYGI GPRTTWTTVTRDLLTDLRKGIGLSNTKAVKATKTMPRRVV KLVVHGTGTIDNITISTTSHMAAFYAASDWLVRNQDERGG WPIMVTRKLGEGFRALEPGWYSAMAQGQAMSTLVRAYLMT KDDRYLKAALRATGPFKLPSEQHGVKAVFMNKYDWYEEYP TIPSSFVLNGFIYSLIGLFDLAQTAGEKLGRDAGQLYSKG MESLKVMLPLYDTGSGTIYDLRHFILGTAPNLARWDYHTT HINQLQLLGTIDNSPIFRDSVKRWKSYLKGGRAKHN B:  VRYEEIDCLINDDATIKGRREGSEVYMPFSWMEKYFEVYG KVVQYDGYDRFEFSHSYSKVYAQREQYHPNGVFMSFEGYN VEVRDRVKCISGVEGVPLSTQWGPQGYFYAIQIAQYGLSH YSKNLTERPPHVEVYDTAEERDSRSSAWTVPKGCSLTRVY DKTRATSVREFSAPENSEGVSLPLGNTKDFIISFDLKFTS NGSVSVILETTEKGPPFVIHYVTTTQLILLKDRDITYGIG PRTTWTTVTRDLLTDLRKGIGLSNTKAVKATKTMPRRVVK LVVHGTGTIDNITISTTSHMAAFYAASDWLVRNQDERGGW PIMVTRKLGEGFRALEPGWYSAMAQGQAMSTLVRAYLMTK DDRYLKAALRATGPFKLPSEQHGVKAVFMNKYDWYEEYPT IPSSFVLNGFIYSLIGLFDLAQTAGEKLGRDAGQLYSKGM ESLKVMLPLYDTGSGTIYDLRHFILGTAPNLARWDYHTTH INQLQLLGTIDNSPIFRDSVKRWKSYLKGGRAKHN Description Functional site 1) chain A residue 150 type BINDING sequence N description BINDING => ECO:0007744|PDB:4PXQ source Swiss-Prot : SWS_FT_FI4 2) chain B residue 155 type BINDING sequence D description BINDING => ECO:0007744|PDB:4PXQ source Swiss-Prot : SWS_FT_FI4 3) chain B residue 183 type BINDING sequence I description BINDING => ECO:0007744|PDB:4PXQ source Swiss-Prot : SWS_FT_FI4 4) chain B residue 398 type BINDING sequence L description BINDING => ECO:0007744|PDB:4PXQ source Swiss-Prot : SWS_FT_FI4 5) chain B residue 483 type BINDING sequence S description BINDING => ECO:0007744|PDB:4PXQ source Swiss-Prot : SWS_FT_FI4 6) chain B residue 532 type BINDING sequence H description BINDING => ECO:0007744|PDB:4PXQ source Swiss-Prot : SWS_FT_FI4 7) chain B residue 544 type BINDING sequence W description BINDING => ECO:0007744|PDB:4PXQ source Swiss-Prot : SWS_FT_FI4 8) chain B residue 568 type BINDING sequence D description BINDING => ECO:0007744|PDB:4PXQ source Swiss-Prot : SWS_FT_FI4 9) chain A residue 155 type BINDING sequence D description BINDING => ECO:0007744|PDB:4PXQ source Swiss-Prot : SWS_FT_FI4 10) chain A residue 183 type BINDING sequence I description BINDING => ECO:0007744|PDB:4PXQ source Swiss-Prot : SWS_FT_FI4 11) chain A residue 398 type BINDING sequence L description BINDING => ECO:0007744|PDB:4PXQ source Swiss-Prot : SWS_FT_FI4 12) chain A residue 483 type BINDING sequence S description BINDING => ECO:0007744|PDB:4PXQ source Swiss-Prot : SWS_FT_FI4 13) chain A residue 532 type BINDING sequence H description BINDING => ECO:0007744|PDB:4PXQ source Swiss-Prot : SWS_FT_FI4 14) chain A residue 544 type BINDING sequence W description BINDING => ECO:0007744|PDB:4PXQ source Swiss-Prot : SWS_FT_FI4 15) chain A residue 568 type BINDING sequence D description BINDING => ECO:0007744|PDB:4PXQ source Swiss-Prot : SWS_FT_FI4 16) chain B residue 150 type BINDING sequence N description BINDING => ECO:0007744|PDB:4PXQ source Swiss-Prot : SWS_FT_FI4 17) chain A residue 208 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:O94923 source Swiss-Prot : SWS_FT_FI5 18) chain A residue 210 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:O94923 source Swiss-Prot : SWS_FT_FI5 19) chain A residue 237 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:O94923 source Swiss-Prot : SWS_FT_FI5 20) chain A residue 361 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:O94923 source Swiss-Prot : SWS_FT_FI5 21) chain B residue 208 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:O94923 source Swiss-Prot : SWS_FT_FI5 22) chain B residue 210 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:O94923 source Swiss-Prot : SWS_FT_FI5 23) chain B residue 237 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:O94923 source Swiss-Prot : SWS_FT_FI5 24) chain B residue 361 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:O94923 source Swiss-Prot : SWS_FT_FI5 25) chain A residue 150 type SITE sequence N description Critical for catalysis => ECO:0000269|PubMed:25568314 source Swiss-Prot : SWS_FT_FI6 26) chain A residue 157 type SITE sequence V description Critical for catalysis => ECO:0000269|PubMed:25568314 source Swiss-Prot : SWS_FT_FI6 27) chain A residue 529 type SITE sequence D description Critical for catalysis => ECO:0000269|PubMed:25568314 source Swiss-Prot : SWS_FT_FI6 28) chain A residue 547 type SITE sequence H description Critical for catalysis => ECO:0000269|PubMed:25568314 source Swiss-Prot : SWS_FT_FI6 29) chain B residue 150 type SITE sequence N description Critical for catalysis => ECO:0000269|PubMed:25568314 source Swiss-Prot : SWS_FT_FI6 30) chain B residue 157 type SITE sequence V description Critical for catalysis => ECO:0000269|PubMed:25568314 source Swiss-Prot : SWS_FT_FI6 31) chain B residue 529 type SITE sequence D description Critical for catalysis => ECO:0000269|PubMed:25568314 source Swiss-Prot : SWS_FT_FI6 32) chain B residue 547 type SITE sequence H description Critical for catalysis => ECO:0000269|PubMed:25568314 source Swiss-Prot : SWS_FT_FI6

Display surface Download Links