Structure of PDB 6fxt Chain A

Receptor sequence
>6fxtA (length=700) Species: 9606 (Homo sapiens) [Search protein sequence]
PVNPEKLLVITVATAETEGYLRFLRSAEFFNYTVRTLGLGEEWRGGDVAR
TVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDVILAGSPTELLKKFVQS
GSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIVRQ
WKYKDDDDDQLFYTRLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLK
FDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLGNYVPNGWTPEGGCGFC
NQDRQPPPRVFLAVFVEQPTPFLPRFLQRLLLLDYPPDRVTLFLHNNEVF
HEPHIADSWPQLQDHFSAVKLVGPEEALSPGEARDMAMDLCRQDPECEFY
FSLDADAVLTNLQTLRILIEENRKVIAPMLSRHGKLWSNFWGALSPDEYY
ARSEDYVELVQRKRVGVWNVPYISQAYVIRGDTLRMELPQRDVFSGSDTD
PDMAFCKSFRDKGIFLHLSNQHEFGRLLATSRYDTEHLHPDLWQIFDNPV
DWKEQYIHENYSRALEGEGIVEQPCPDVYWFPLLSEQMCDELVAEMEHYG
QWSGGRHEDSRLAGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTESL
FPGYHTKARAVMNFVVRYRPDEQPSLRPHHDSSTFTLNVALNHKGLDYEG
GGCRFLRYDCVISSPRKGWALLHPGRLTHYHEGLPTTWGTRYIMVSFVDP
3D structure
PDB6fxt Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3.
ChainA
Resolution2.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.11.4: procollagen-lysine 5-dioxygenase.
2.4.1.50: procollagen galactosyltransferase.
2.4.1.66: procollagen glucosyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 AKG A R599 Y656 L664 H667 H719 R729 F735 R561 Y618 L626 H629 H681 R691 F697
BS02 UDP A V44 A45 T46 W75 D112 S113 Y114 D115 H253 K259 V12 A13 T14 W43 D80 S81 Y82 D83 H221 K227
BS03 FE2 A H667 D669 H719 H629 D631 H681
BS04 FE2 A H595 D597 D611 H613 H557 D559 D573 H575
BS05 MN A D112 D115 H253 D80 D83 H221
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0008475 procollagen-lysine 5-dioxygenase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0016757 glycosyltransferase activity
GO:0031418 L-ascorbic acid binding
GO:0033823 procollagen glucosyltransferase activity
GO:0036094 small molecule binding
GO:0046872 metal ion binding
GO:0050211 procollagen galactosyltransferase activity
GO:0051213 dioxygenase activity
Biological Process
GO:0001701 in utero embryonic development
GO:0001886 endothelial cell morphogenesis
GO:0006493 protein O-linked glycosylation
GO:0008104 protein localization
GO:0017185 peptidyl-lysine hydroxylation
GO:0021915 neural tube development
GO:0030199 collagen fibril organization
GO:0032963 collagen metabolic process
GO:0042311 vasodilation
GO:0046947 hydroxylysine biosynthetic process
GO:0048730 epidermis morphogenesis
GO:0060425 lung morphogenesis
GO:0070831 basement membrane assembly
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005783 endoplasmic reticulum
GO:0005788 endoplasmic reticulum lumen
GO:0005789 endoplasmic reticulum membrane
GO:0005791 rough endoplasmic reticulum
GO:0005794 Golgi apparatus
GO:0005802 trans-Golgi network
GO:0016020 membrane
GO:0062023 collagen-containing extracellular matrix
GO:0070062 extracellular exosome

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6fxt, PDBe:6fxt, PDBj:6fxt
PDBsum6fxt
PubMed30089812
UniProtO60568|PLOD3_HUMAN Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3 (Gene Name=PLOD3)

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