Structure of PDB 5nrf Chain A

Receptor sequence
>5nrfA (length=377) Species: 9606 (Homo sapiens) [Search protein sequence]
AKLVCYFTNWAQYRQGEARFLPKDLDPSLCTHLIYAFAGMTNHQLSTTEW
NDETLYQEFNGLKKMNPKLKTLLAIGGWNFGTQKFTDMVATANNRQTFVN
SAIRFLRKYSFDGLDLDWEYPGSQGSPAVDKERFTTLVQDLANAFQQEAQ
TSGKERLLLSAAVPAGQTYVDAGYEVDKIAQNLDFVNLMAYDFHGSWEKV
TGHNSPLYKRQEESGAAASLNVDAAVQQWLQKGTPASKLILGMPTYGRSF
TLASSSDTRVGAPATGSGTPGPFTKEGGMLAYYEVCSWKGATKQRIQDQK
VPYIFRDNQWVGFDDVESFKTKVSYLKQKGLGGAMVWALDLDDFAGFSCN
QGRYPLIQTLRQELSLVPRGSHHHHHH
3D structure
PDB5nrf Targeting Acidic Mammalian chitinase Is Effective in Animal Model of Asthma.
ChainA
Resolution1.447 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D136 D138 E140 Y212
Catalytic site (residue number reindexed from 1) D115 D117 E119 Y191
Enzyme Commision number 3.2.1.14: chitinase.
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 95Q A Y27 W99 A183 M210 Y212 D213 Y267 R269 T295 E297 M300 M356 W358 Y6 W78 A162 M189 Y191 D192 Y246 R248 T274 E276 M279 M335 W337 MOAD: ic50=163nM
PDBbind-CN: -logKd/Ki=6.79,IC50=163nM
BindingDB: IC50=163nM
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008061 chitin binding
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:5nrf, PDBe:5nrf, PDBj:5nrf
PDBsum5nrf
PubMed29283260
UniProtQ13231|CHIT1_HUMAN Chitotriosidase-1 (Gene Name=CHIT1)

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