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2Y8U

A. nidulans chitin deacetylase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004099molecular_functionchitin deacetylase activity
A0005575cellular_componentcellular_component
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0006032biological_processchitin catabolic process
A0008061molecular_functionchitin binding
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0046872molecular_functionmetal ion binding
A0071555biological_processcell wall organization
B0000272biological_processpolysaccharide catabolic process
B0004099molecular_functionchitin deacetylase activity
B0005575cellular_componentcellular_component
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0006032biological_processchitin catabolic process
B0008061molecular_functionchitin binding
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0046872molecular_functionmetal ion binding
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 1238
ChainResidue
AASP47
AASP48
AHIS97
AHIS101
ATYR138
AHIS196
ACO1239
AHOH2007
AHOH2061

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 1239
ChainResidue
AASP48
AHIS97
AHIS101
APO41238
AHOH2007

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA A 1240
ChainResidue
AGLY189

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 1241
ChainResidue
ATHR34
ANA1244
AHOH2003

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1242
ChainResidue
APHE179

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 1244
ChainResidue
ATHR34
APRO125
ANA1241

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 1238
ChainResidue
BASP47
BASP48
BHIS97
BHIS101
BTYR138
BHIS196
BCO1239
BHOH2057

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO B 1239
ChainResidue
BASP48
BHIS97
BHIS101
BPO41238

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 1240
ChainResidue
BARG118
BHOH2029

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01014
ChainResidueDetails
AASP47
BASP47

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01014
ChainResidueDetails
AHIS196
BHIS196

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q6DWK3
ChainResidueDetails
AASP47
ATYR138
BASP47
BTYR138

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01014
ChainResidueDetails
AASP48
AHIS97
AHIS101
BASP48
BHIS97
BHIS101

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: May prevent de-N-acetylated sugar residues from interacting with the active site => ECO:0000303|PubMed:28496100
ChainResidueDetails
ALYS164
BLYS164

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN176
BASN176

224004

PDB entries from 2024-08-21

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