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6FXK

Crystal Structure of full-length Human Lysyl Hydroxylase LH3

Functional Information from GO Data
ChainGOidnamespacecontents
A0001701biological_processin utero embryonic development
A0001886biological_processendothelial cell morphogenesis
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
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
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
A0062023cellular_componentcollagen-containing extracellular matrix
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 Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:30089812, ECO:0007744|PDB:6FXY
ChainResidueDetails
AVAL44
AASP112
AASP115
AHIS253
AGLY256
AARG599
ATYR656
AASN676
AARG729

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:30089812, ECO:0007744|PDB:6FXY
ChainResidueDetails
AHIS667
AASP669
AHIS719

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:30089812, ECO:0007744|PDB:6FXY
ChainResidueDetails
AASN63
AASN548

226707

PDB entries from 2024-10-30

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