Structure of PDB 6fxr Chain A

Receptor sequence

>6fxrA (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

PDB

6fxr Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3.

Chain

Resolution

2.1 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)
BS01	AKG	A	R599 Y656 L664 H667 N676 C691 H719 R729 I731	R561 Y618 L626 H629 N638 C653 H681 R691 I693
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

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Biological Process

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Cellular Component

External links

PDB	RCSB:6fxr, PDBe:6fxr, PDBj:6fxr
PDBsum	6fxr
PubMed	30089812
UniProt	O60568\|PLOD3_HUMAN Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3 (Gene Name=PLOD3)

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