Structure of PDB 1hkk Chain A

Receptor sequence
>1hkkA (length=364) Species: 9606 (Homo sapiens) [Search protein sequence]
AKLVCYFTNWAQYRQGEARFLPKDLDPSLCTHLIYAFAGMTNHQLSTTEW
NDETLYQEFNGLKKMNPKLKTLLAIGGWNFGTQKFTDMVATANNRQTFVN
SAIRFLRKYSFDGLDLDWEYPGSQGSPAVDKERFTTLVQDLANAFQQEAQ
TSGKERLLLSAAVPAGQTYVDAGYEVDKIAQNLDFVNLMAYDFHGSWEKV
TGHNSPLYKRQEQSGAAASLNVDAAVQQWLQKGTPASKLILGMPTYGRSF
TLASSSDTRVGAPATGSGTPGPFTKEGGMLAYYEVCSWKGATKQRIQDQK
VPYIFRDNQWVGFDDVESFKTKVSYLKQKGLGGAMVWALDLDDFAGFSCN
QGRYPLIQTLRQEL
3D structure
PDB1hkk Crystal Structures of Allosamidin Derivatives in Complex with Human Macrophage Chitinase.
ChainA
Resolution1.85 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 AMI A Y27 W99 D138 E140 M210 Y212 D213 Y267 W358 Y6 W78 D117 E119 M189 Y191 D192 Y246 W337 PDBbind-CN: -logKd/Ki=7.40,IC50=40nM
BS02 AMI A Y141 Q145 A186 G187 Y190 D213 Y120 Q124 A165 G166 Y169 D192 PDBbind-CN: -logKd/Ki=7.40,IC50=40nM
BS03 ZN A H215 E219 H194 E198
BS04 ZN A H64 D108 H43 D87
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:1hkk, PDBe:1hkk, PDBj:1hkk
PDBsum1hkk
PubMed12639956
UniProtQ13231|CHIT1_HUMAN Chitotriosidase-1 (Gene Name=CHIT1)

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