Structure of PDB 1ll4 Chain A

Receptor sequence
>1ll4A (length=392) Species: 5501 (Coccidioides immitis) [Search protein sequence]
GGFRSVVYFVNWAIYGRGHNPQDLKADQFTHILYAFANIRPSGEVYLSDT
WADTDKHYPGDKWDEPGNNVYGCIKQMYLLKKNNRNLKTLLSIGGWTYSP
NFKTPASTEEGRKKFADTSLKLMKDLGFDGIDIDWEYPEDEKQANDFVLL
LKACREALDAYSAKHPNGKKFLLTIASPAGPQNYNKLKLAEMDKYLDFWN
LMAYDFSGSWDKVSGHMSNVFPSTTKPESTPFSSDKAVKDYIKAGVPANK
IVLGMPLYGRAFASTDGIGTSFNGVGGGSWENGVWDYKDMPQQGAQVTEL
EDIAASYSYDKNKRYLISYDTVKIAGKKAEYITKNGMGGGMWWESSSDKT
GNESLVGTVVNGLGGTGKLEQRENELSYPESVYDNLKNGMPS
3D structure
PDB1ll4 THE STRUCTURE OF AN ALLOSAMIDIN COMPLEX WITH THE Coccidioides IMMITIS CHITINASE DEFINES A ROLE FOR A SECOND ACID RESIDUE IN SUBSTRATE-ASSISTED MECHANISM
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D167 D169 E171 Y239
Catalytic site (residue number reindexed from 1) D132 D134 E136 Y204
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 Y43 F71 D169 E171 M237 Y239 D240 Y293 W378 Y8 F36 D134 E136 M202 Y204 D205 Y258 W343 PDBbind-CN: -logKd/Ki=7.22,Ki=60nM
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004568 chitinase activity
GO:0008061 chitin binding
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0005975 carbohydrate metabolic process
GO:0006032 chitin catabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ll4, PDBe:1ll4, PDBj:1ll4
PDBsum1ll4
PubMed12079386
UniProtP0CB51|CHI1_COCPS Endochitinase 1 (Gene Name=CTS1)

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