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5KZD

N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus with bound sialic acid alditol

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0008747molecular_functionN-acetylneuraminate lyase activity
A0016829molecular_functionlyase activity
A0019262biological_processN-acetylneuraminate catabolic process
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0008747molecular_functionN-acetylneuraminate lyase activity
B0016829molecular_functionlyase activity
B0019262biological_processN-acetylneuraminate catabolic process
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005975biological_processcarbohydrate metabolic process
C0008747molecular_functionN-acetylneuraminate lyase activity
C0016829molecular_functionlyase activity
C0019262biological_processN-acetylneuraminate catabolic process
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005975biological_processcarbohydrate metabolic process
D0008747molecular_functionN-acetylneuraminate lyase activity
D0016829molecular_functionlyase activity
D0019262biological_processN-acetylneuraminate catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue RCJ A 301
ChainResidue
AALA11
AILE206
AGLY207
ASER208
AILE243
AILE251
ATYR252
ATYR44
AGLY47
ASER48
ASER49
ALYS165
AGLY189
AASP191
AGLU192

site_idAC2
Number of Residues15
Detailsbinding site for residue RCJ B 301
ChainResidue
BALA11
BTYR44
BGLY47
BSER48
BSER49
BLYS165
BGLY189
BASP191
BGLU192
BILE206
BGLY207
BSER208
BLEU247
BILE251
BTYR252

site_idAC3
Number of Residues14
Detailsbinding site for residue RCJ C 301
ChainResidue
CALA11
CTYR44
CGLY47
CSER48
CSER49
CTYR137
CLYS165
CGLY189
CASP191
CGLU192
CGLY207
CSER208
CILE251
CTYR252

site_idAC4
Number of Residues16
Detailsbinding site for residue RCJ D 301
ChainResidue
DALA11
DTYR44
DGLY47
DSER48
DSER49
DTYR137
DLYS165
DGLY189
DASP191
DGLU192
DILE206
DGLY207
DSER208
DLEU247
DILE251
DTYR252

Functional Information from PROSITE/UniProt
site_idPS00666
Number of Residues31
DetailsDHDPS_2 Dihydrodipicolinate synthase signature 2. YAIPdlTgvnIsieqfselfnhek.IvGVKYT
ChainResidueDetails
ATYR137-THR167

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01237","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"HAMAP-Rule","id":"MF_01237","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23418011","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27943302","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5KZD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01237","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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