Structure of PDB 4kgj Chain A

Receptor sequence
>4kgjA (length=595) Species: 9606 (Homo sapiens) [Search protein sequence]
APHLVQVDAARALWPLRRFWRSTGFCPPYVLSWDQQLNLAYVGAVPHRGI
KQVRTHWLLELVTTLSYNFTHLDGYLDLLRENQLLPGFELMGSASGHFTD
FEDKQQVFEWKDLVSSLARRYIGRYGLAHVSKWNFETWNEPDHHDFDNVS
MTMQGFLNYYDACSEGLRAASPALRLGGPGDSFHTPPRSPLSWGLLRHCH
DGTNFFTGEAGVRLDYISLHRKGARSSISILEQEKVVAQQIRQLFPKFAD
TPIYNDEADPLVGWSLPQPWRADVTYAAMVVKVIAQHQNLLLANTTSAFP
YALLSNDNAFLSYHPHPFAQRTLTARFQVNNTRPPHVQLLRKPVLTAMGL
LALLDEEQLWAEVSQAGTVLDSNHTVGVLASAHRPQGPADAWRAAVLIYA
SDDTRAHPNRSVAVTLRLRGVPPGPGLVYVTRYLDNGLCSPDGEWRRLGR
PVFPTAEQFRRMRAAEDPVAAAPRPLPAGGRLTLRPALRLPSLLLVHVCA
RPEKPPGQVTRLRALPLTQGQLVLVWSDEHVGSKCLWTYEIQFSQDYTPV
SRKPSTFNLFVFSPDTGAVSGSYRVRALDYWARPGPFSDPVPYLE
3D structure
PDB4kgj Insights into mucopolysaccharidosis I from the structure and action of alpha-L-iduronidase.
ChainA
Resolution2.99 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.76: L-iduronidase.
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 IDF A H91 E182 K264 E299 V304 G305 W306 D349 R363 H56 E140 K222 E257 V262 G263 W264 D307 R321
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4kgj, PDBe:4kgj, PDBj:4kgj
PDBsum4kgj
PubMed24036510
UniProtP35475|IDUA_HUMAN Alpha-L-iduronidase (Gene Name=IDUA)

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