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4LY4

Crystal structure of peptidoglycan deacetylase (HP0310) with Zinc from Helicobacter pylori

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0005975biological_processcarbohydrate metabolic process
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0045493biological_processxylan catabolic process
A0046555molecular_functionacetylxylan esterase activity
A0046872molecular_functionmetal ion binding
A0071555biological_processcell wall organization
B0000272biological_processpolysaccharide catabolic process
B0005975biological_processcarbohydrate metabolic process
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0045493biological_processxylan catabolic process
B0046555molecular_functionacetylxylan esterase activity
B0046872molecular_functionmetal ion binding
B0071555biological_processcell wall organization
C0000272biological_processpolysaccharide catabolic process
C0005975biological_processcarbohydrate metabolic process
C0016787molecular_functionhydrolase activity
C0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
C0045493biological_processxylan catabolic process
C0046555molecular_functionacetylxylan esterase activity
C0046872molecular_functionmetal ion binding
C0071555biological_processcell wall organization
D0000272biological_processpolysaccharide catabolic process
D0005975biological_processcarbohydrate metabolic process
D0016787molecular_functionhydrolase activity
D0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
D0045493biological_processxylan catabolic process
D0046555molecular_functionacetylxylan esterase activity
D0046872molecular_functionmetal ion binding
D0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AASP12
AASP14
AHIS86
AHIS90

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BASP14
BHIS86
BHIS90
BHOH401

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN C 301
ChainResidue
CHIS86
CHIS90
CASP14

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 301
ChainResidue
DASP14
DHIS86
DHIS90
DHOH401

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues988
DetailsDomain: {"description":"NodB homology","evidences":[{"source":"PROSITE-ProRule","id":"PRU01014","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21559431","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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