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4DYG

Crystal Structure of a Family GH-19 Chitinase from rye seeds in complex with (GlcNAc)4

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004568molecular_functionchitinase activity
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0006032biological_processchitin catabolic process
A0008061molecular_functionchitin binding
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0031640biological_processkilling of cells of another organism
A0050832biological_processdefense response to fungus
B0000272biological_processpolysaccharide catabolic process
B0004568molecular_functionchitinase activity
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0006032biological_processchitin catabolic process
B0008061molecular_functionchitin binding
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016998biological_processcell wall macromolecule catabolic process
B0031640biological_processkilling of cells of another organism
B0050832biological_processdefense response to fungus
Functional Information from PROSITE/UniProt
site_idPS00773
Number of Residues23
DetailsCHITINASE_19_1 Chitinases family 19 signature 1. Cqakg.FYTydaFVaAanaFpgFG
ChainResidueDetails
ACYS23-GLY45

site_idPS00774
Number of Residues11
DetailsCHITINASE_19_2 Chitinases family 19 signature 2. VSFkTALWFWM
ChainResidueDetails
AVAL149-MET159

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P29022
ChainResidueDetails
AGLU67
BGLU67

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: May be involved in substrate-binding => ECO:0000269|Ref.5
ChainResidueDetails
ATRP72
BTRP72

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: May be involved in substrate-binding => ECO:0000269|PubMed:9532801
ChainResidueDetails
AASP95
BASP95

222624

PDB entries from 2024-07-17

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