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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
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01237
ChainResidueDetails
ATYR137
BTYR137
CTYR137
DTYR137

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_01237, ECO:0000269|PubMed:23418011
ChainResidueDetails
ALYS165
BLYS165
CLYS165
DLYS165

site_idSWS_FT_FI3
Number of Residues28
DetailsBINDING: BINDING => ECO:0000305|PubMed:27943302, ECO:0007744|PDB:5KZD
ChainResidueDetails
ASER48
BASP191
BGLU192
BSER208
CSER48
CSER49
CGLY189
CASP191
CGLU192
CSER208
DSER48
ASER49
DSER49
DGLY189
DASP191
DGLU192
DSER208
ATYR252
BTYR252
CTYR252
DTYR252
AGLY189
AASP191
AGLU192
ASER208
BSER48
BSER49
BGLY189

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01237
ChainResidueDetails
ATHR167
BTHR167
CTHR167
DTHR167

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PDB entries from 2024-10-30

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