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5ZJM

Crystal structure of N-acetylneuraminate lyase from Fusobacterium nucleatum

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 Residues5
Detailsbinding site for residue EDO A 301
ChainResidue
AASN13
AILE18
AASN19
AGLU20
ALYS21

site_idAC2
Number of Residues5
Detailsbinding site for residue EDO B 301
ChainResidue
BLYS21
BASN13
BILE18
BASN19
BGLU20

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO C 301
ChainResidue
CASN13
CILE18
CASN19
CGLU20
CLYS21

Functional Information from PROSITE/UniProt
site_idPS00665
Number of Residues18
DetailsDHDPS_1 Dihydrodipicolinate synthase signature 1. GLYvgGSTGENfmisteE
ChainResidueDetails
AGLY38-GLU55

site_idPS00666
Number of Residues31
DetailsDHDPS_2 Dihydrodipicolinate synthase signature 2. YSIPflTgvnMslsqfgelfenek.IiGVKFT
ChainResidueDetails
ATYR133-THR163

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01237
ChainResidueDetails
ATYR133
BTYR133
CTYR133
DTYR133

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_01237, ECO:0000305|PubMed:30387778
ChainResidueDetails
ALYS161
BLYS161
CLYS161
DLYS161

site_idSWS_FT_FI3
Number of Residues28
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01237
ChainResidueDetails
ASER44
BTHR163
BGLY185
BASP187
BGLU188
BSER204
CSER44
CTHR45
CTHR163
CGLY185
CASP187
ATHR45
CGLU188
CSER204
DSER44
DTHR45
DTHR163
DGLY185
DASP187
DGLU188
DSER204
ATHR163
AGLY185
AASP187
AGLU188
ASER204
BSER44
BTHR45

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PDB entries from 2024-09-04

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