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2C1I

Structure of Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) D 275 N Mutant.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0005975biological_processcarbohydrate metabolic process
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0042545biological_processcell wall modification
A0046872molecular_functionmetal ion binding
A0050119molecular_functionN-acetylglucosamine deacetylase activity
A0060241molecular_functionlysozyme inhibitor activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1465
ChainResidue
AASP276
AHIS326
AHIS330
ASO41467

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1466
ChainResidue
AGLU144
AGLU146
AGLU340
AHOH2209

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A1467
ChainResidue
AASP276
AHIS326
AHIS330
APRO366
ATYR367
AHIS417
AMES1464
AZN1465
AHOH2210
AHOH2211
AASN275

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MES A1464
ChainResidue
ATYR367
ATRP385
AASP388
ATRP392
ASO41467

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:16221761
ChainResidueDetails
AASN275

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:16221761
ChainResidueDetails
AHIS417

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16221761
ChainResidueDetails
AASP276
AHIS326
AHIS330
ATYR367

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Raises pKa of active site His => ECO:0000269|PubMed:16221761
ChainResidueDetails
AASP391

221051

PDB entries from 2024-06-12

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