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3QBU

Crystal structure of putative peptidoglycan deactelyase (HP0310) from Helicobacter pylori

Functional Information from GO Data
ChainGOidnamespacecontents
A0005975biological_processcarbohydrate metabolic process
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0046555molecular_functionacetylxylan esterase activity
B0005975biological_processcarbohydrate metabolic process
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0046555molecular_functionacetylxylan esterase activity
C0005975biological_processcarbohydrate metabolic process
C0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
C0046555molecular_functionacetylxylan esterase activity
D0005975biological_processcarbohydrate metabolic process
D0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
D0046555molecular_functionacetylxylan esterase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 294
ChainResidue
AASP14
AHIS86
AHIS90
AHOH295
AHOH686

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 294
ChainResidue
BASP14
BHIS86
BHIS90
BHOH759

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN C 294
ChainResidue
CASP14
CHIS86
CHIS90
CHOH386
CHOH689

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 294
ChainResidue
DASP14
DHIS86
DHIS90
DHOH429

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

252091

PDB entries from 2026-04-15

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