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6TEZ

Crystal Structure of full-length Human Lysyl Hydroxylase LH3 - Val80Lys mutant - Cocrystal with Fe2+, Mn2+, UDP-Glucuronic Acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0001701biological_processin utero embryonic development
A0001886biological_processendothelial cell morphogenesis
A0003824molecular_functioncatalytic activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0005789cellular_componentendoplasmic reticulum membrane
A0005791cellular_componentrough endoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0005802cellular_componenttrans-Golgi network
A0006493biological_processprotein O-linked glycosylation
A0008104biological_processprotein localization
A0008475molecular_functionprocollagen-lysine 5-dioxygenase activity
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0017185biological_processpeptidyl-lysine hydroxylation
A0021915biological_processneural tube development
A0030199biological_processcollagen fibril organization
A0031418molecular_functionL-ascorbic acid binding
A0032963biological_processcollagen metabolic process
A0033823molecular_functionprocollagen glucosyltransferase activity
A0036094molecular_functionsmall molecule binding
A0042311biological_processvasodilation
A0046872molecular_functionmetal ion binding
A0046947biological_processhydroxylysine biosynthetic process
A0048730biological_processepidermis morphogenesis
A0050211molecular_functionprocollagen galactosyltransferase activity
A0051213molecular_functiondioxygenase activity
A0060425biological_processlung morphogenesis
A0070062cellular_componentextracellular exosome
A0070831biological_processbasement membrane assembly
Functional Information from PROSITE/UniProt
site_idPS01325
Number of Residues8
DetailsLYS_HYDROXYLASE Lysyl hydroxylase signature. PHHDSSTF
ChainResidueDetails
APRO666-PHE673

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues91
DetailsDomain: {"description":"Fe2OG dioxygenase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues225
DetailsRegion: {"description":"Accessory region","evidences":[{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues43
DetailsRegion: {"description":"Important for dimerization","evidences":[{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6FXY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6FXY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6FXY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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