eF-site ID 6fxx-A PDB Code 6fxx Chain A click to enlarge Title Crystal Structure of full-length Human Lysyl Hydroxylase LH3 - Cocrystal with Fe2+, Mn2+, UDP-Gal, Hg2+ Soak Classification TRANSFERASE Compound Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 Source (PLOD3_HUMAN) Sequence A:  PVNPEKLLVITVATAETEGYLRFLRSAEFFNYTVRTLGLG EEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVD SYDVILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAE QYPEVGTGKRFLNSGGFIGFATTIHQIVRQWKYKDDDDDQ LFYTRLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLK FDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLGNYVPNG WTPEGGCGFCNQDRQPPPRVFLAVFVEQPTPFLPRFLQRL LLLDYPPDRVTLFLHNNEVFHEPHIADSWPQLQDHFSAVK LVGPEEALSPGEARDMAMDLCRQDPECEFYFSLDADAVLT NLQTLRILIEENRKVIAPMLSRHGKLWSNFWGALSPDEYY ARSEDYVELVQRKRVGVWNVPYISQAYVIRGDTLRMELPQ RDVFSGSDTDPDMAFCKSFRDKGIFLHLSNQHEFGRLLAT SRYDTEHLHPDLWQIFDNPVDWKEQYIHENYSRALEGEGI VEQPCPDVYWFPLLSEQMCDELVAEMEHYGQWSGGRHEDS RLAGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTESL FPGYHTKARAVMNFVVRYRPDEQPSLRPHHDSSTFTLNVA LNHKGLDYEGGGCRFLRYDCVISSPRKGWALLHPGRLTHY HEGLPTTWGTRYIMVSFVDP Description (1)  Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 (E.C.1.14.11.4) Functional site 1) chain A residue 666-673 type prosite sequence PHHDSSTF description LYS_HYDROXYLASE Lysyl hydroxylase signature. PHHDSSTF source prosite : PS01325 2) chain A residue 253 type BINDING sequence H description BINDING => ECO:0000269|PubMed:30089812, ECO:0007744|PDB:6FXY source Swiss-Prot : SWS_FT_FI1 3) chain A residue 256 type BINDING sequence G description BINDING => ECO:0000269|PubMed:30089812, ECO:0007744|PDB:6FXY source Swiss-Prot : SWS_FT_FI1 4) chain A residue 599 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30089812, ECO:0007744|PDB:6FXY source Swiss-Prot : SWS_FT_FI1 5) chain A residue 656 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:30089812, ECO:0007744|PDB:6FXY source Swiss-Prot : SWS_FT_FI1 6) chain A residue 676 type BINDING sequence N description BINDING => ECO:0000269|PubMed:30089812, ECO:0007744|PDB:6FXY source Swiss-Prot : SWS_FT_FI1 7) chain A residue 729 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30089812, ECO:0007744|PDB:6FXY source Swiss-Prot : SWS_FT_FI1 8) chain A residue 44 type BINDING sequence V description BINDING => ECO:0000269|PubMed:30089812, ECO:0007744|PDB:6FXY source Swiss-Prot : SWS_FT_FI1 9) chain A residue 112 type BINDING sequence D description BINDING => ECO:0000269|PubMed:30089812, ECO:0007744|PDB:6FXY source Swiss-Prot : SWS_FT_FI1 10) chain A residue 115 type BINDING sequence D description BINDING => ECO:0000269|PubMed:30089812, ECO:0007744|PDB:6FXY source Swiss-Prot : SWS_FT_FI1 11) chain A residue 667 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:30089812, ECO:0007744|PDB:6FXY source Swiss-Prot : SWS_FT_FI2 12) chain A residue 669 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:30089812, ECO:0007744|PDB:6FXY source Swiss-Prot : SWS_FT_FI2 13) chain A residue 719 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:30089812, ECO:0007744|PDB:6FXY source Swiss-Prot : SWS_FT_FI2 14) chain A residue 63 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:30089812, ECO:0007744|PDB:6FXY source Swiss-Prot : SWS_FT_FI3 15) chain A residue 548 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:30089812, ECO:0007744|PDB:6FXY source Swiss-Prot : SWS_FT_FI3

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