Structure of PDB 6fxm Chain A Binding Site BS04

Receptor Information
>6fxm Chain A (length=679) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PVNPEKLLVITVATAETEGYLRFLRSAEFFNYTVRTLGLGGGQKVRWLKK
EMEKYADREDMIIMFVDSYDVILAGSPTELLKKFVQSGSRLLFSAESFCW
PEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIVRQWKYKDDDDDQLFY
TRLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRIRNVAY
DTLPIVVHGNGPTKLQLNYLGNYVPNGWTPEGGCGFCNQDRRQPPPRVFL
AVFVEQPTPFLPRFLQRLLLLDYPPDRVTLFLHNNEVFHEPHIADSWPQL
QDHFSAVKLVGPEEALSPGEARDMAMDLCRQDPECEFYFSLDADAVLTNL
QTLRILIEENRKVIAPMLSRHGKLWSNFWGALSPDEYYARSEDYVELVQR
KRVGVWNVPYISQAYVIRGDTLRMELPQRDVFSGSDTDPDMAFCKSFRDK
GIFLHLSNQHEFGRLLATSRYDTEHLHPDLWQIFDNPVDWKEQYIHENYS
RALEGEGIVEQPCPDVYWFPLLSEQMCDELVAEMEHYGQWSDSRLAGVPT
VDIHMKQVGYEDQWLQLLRTYVGPMTESLFPGYHTKARAVMNFVVRYRPD
EQPSLRPHHDSSTFTLNVALNHKGLDYEGGGCRFLRYDCVISSPRKGWAL
LHPGRLTHYHEGLPTTWGTRYIMVSFVDP
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain6fxm Chain A Residue 808 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6fxm Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		D597 D611 H613
Binding residue
(residue number reindexed from 1)		D542 D552 H554
Annotation score1
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.
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6fxm, PDBe:6fxm, PDBj:6fxm
PDBsum6fxm
PubMed30089812
UniProtO60568|PLOD3_HUMAN Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3 (Gene Name=PLOD3)

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