Structure of PDB 1hkj Chain A

Receptor sequence
>1hkjA (length=365) Species: 9606 (Homo sapiens) [Search protein sequence]
AKLVCYFTNWAQYRQGEARFLPKDLDPSLCTHLIYAFAGMTNHQLSTTEW
NDETLYQEFNGLKKMNPKLKTLLAIGGWNFGTQKFTDMVATANNRQTFVN
SAIRFLRKYSFDGLDLDWEYPGSQGSPAVDKERFTTLVQDLANAFQQEAQ
TSGKERLLLSAAVPAGQTYVDAGYEVDKIAQNLDFVNLMAYDFHGSWEKV
TGHNSPLYKRQEQSGAAASLNVDAAVQQWLQKGTPASKLILGMPTYGRSF
TLASSSDTRVGAPATGSGTPGPFTKEGGMLAYYEVCSWKGATKQRIQDQK
VPYIFRDNQWVGFDDVESFKTKVSYLKQKGLGGAMVWALDLDDFAGFSCN
QGRYPLIQTLRQELS
3D structure
PDB1hkj Crystal Structures of Allosamidin Derivatives in Complex with Human Macrophage Chitinase
ChainA
Resolution2.6 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 NA1 A W31 N100 E297 W10 N79 E276 PDBbind-CN: -logKd/Ki=8.59,IC50=2.6nM
BS02 AMI A Y27 W99 D138 E140 M210 Y212 Y267 M356 W358 Y6 W78 D117 E119 M189 Y191 Y246 M335 W337 PDBbind-CN: -logKd/Ki=8.59,IC50=2.6nM
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008061 chitin binding
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1hkj, PDBe:1hkj, PDBj:1hkj
PDBsum1hkj
PubMed12639956
UniProtQ13231|CHIT1_HUMAN Chitotriosidase-1 (Gene Name=CHIT1)

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