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2BAA

THE REFINED CRYSTAL STRUCTURE OF AN ENDOCHITINASE FROM HORDEUM VULGARE L. SEEDS TO 1.8 ANGSTROMS RESOLUTION

Replaces:  1BAA
Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004568molecular_functionchitinase activity
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0006032biological_processchitin catabolic process
A0006952biological_processdefense response
A0008843molecular_functionendochitinase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0050832biological_processdefense response to fungus
Functional Information from PROSITE/UniProt
site_idPS00773
Number of Residues23
DetailsCHITINASE_19_1 Chitinases family 19 signature 1. Cqakg.FYTydaFVaAaaaFpgFG
ChainResidueDetails
ACYS23-GLY45

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P29022
ChainResidueDetails
AGLU67

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cns
ChainResidueDetails
ASER120
AGLU67
AGLU89

site_idMCSA1
Number of Residues2
DetailsM-CSA 475
ChainResidueDetails
AGLU67electrostatic stabiliser, proton shuttle (general acid/base)
AGLU89electrostatic stabiliser, proton shuttle (general acid/base)

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PDB entries from 2025-06-25

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