Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1CNS

CRYSTAL STRUCTURE OF CHITINASE AT 1.91A RESOLUTION

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
B0000272biological_processpolysaccharide catabolic process
B0004568molecular_functionchitinase activity
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0006032biological_processchitin catabolic process
B0006952biological_processdefense response
B0008843molecular_functionendochitinase activity
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016998biological_processcell wall macromolecule catabolic process
B0050832biological_processdefense response to fungus
Functional Information from PROSITE/UniProt
site_idPS00773
Number of Residues23
DetailsCHITINASE_19_1 Chitinases family 19 signature 1. Cqakg.FYTydaFVaAaaaFsgFG
ChainResidueDetails
ACYS23-GLY45

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P29022","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 12369923
ChainResidueDetails
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)

site_idMCSA2
Number of Residues2
DetailsM-CSA 475
ChainResidueDetails
BGLU67electrostatic stabiliser, proton shuttle (general acid/base)
BGLU89electrostatic stabiliser, proton shuttle (general acid/base)

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon