Structure of PDB 1hkm Chain A

Receptor sequence
>1hkmA (length=365) Species: 9606 (Homo sapiens) [Search protein sequence]
AKLVCYFTNWAQYRQGEARFLPKDLDPSLCTHLIYAFAGMTNHQLSTTEW
NDETLYQEFNGLKKMNPKLKTLLAIGGWNFGTQKFTDMVATANNRQTFVN
SAIRFLRKYSFDGLDLDWEYPGSQGSPAVDKERFTTLVQDLANAFQQEAQ
TSGKERLLLSAAVPAGQTYVDAGYEVDKIAQNLDFVNLMAYDFHGSWEKV
TGHNSPLYKRQEQSGAAASLNVDAAVQQWLQKGTPASKLILGMPTYGRSF
TLASSSDTRVGAPATGSGTPGPFTKEGGMLAYYEVCSWKGATKQRIQDQK
VPYIFRDNQWVGFDDVESFKTKVSYLKQKGLGGAMVWALDLDDFAGFSCN
QGRYPLIQTLRQELS
3D structure
PDB1hkm Crystal Structures of Allosamidin Derivatives in Complex with Human Macrophage Chitinase
ChainA
Resolution2.55 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 ALI A Y27 W99 D138 E140 M210 Y212 D213 Y267 W358 Y6 W78 D117 E119 M189 Y191 D192 Y246 W337 PDBbind-CN: -logKd/Ki=8.72,IC50=1.9nM
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:1hkm, PDBe:1hkm, PDBj:1hkm
PDBsum1hkm
PubMed12639956
UniProtQ13231|CHIT1_HUMAN Chitotriosidase-1 (Gene Name=CHIT1)

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