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1FDY

N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH HYDROXYPYRUVATE

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
A0042802molecular_functionidentical protein binding
A0044010biological_processsingle-species biofilm formation
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0008747molecular_functionN-acetylneuraminate lyase activity
B0016829molecular_functionlyase activity
B0019262biological_processN-acetylneuraminate catabolic process
B0042802molecular_functionidentical protein binding
B0044010biological_processsingle-species biofilm formation
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005975biological_processcarbohydrate metabolic process
C0008747molecular_functionN-acetylneuraminate lyase activity
C0016829molecular_functionlyase activity
C0019262biological_processN-acetylneuraminate catabolic process
C0042802molecular_functionidentical protein binding
C0044010biological_processsingle-species biofilm formation
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005975biological_processcarbohydrate metabolic process
D0008747molecular_functionN-acetylneuraminate lyase activity
D0016829molecular_functionlyase activity
D0019262biological_processN-acetylneuraminate catabolic process
D0042802molecular_functionidentical protein binding
D0044010biological_processsingle-species biofilm formation
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 3PY A 802
ChainResidue
AALA11
ATYR43
AGLY46
ASER47
ATHR48
ATYR137
ALYS165

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 3PY B 804
ChainResidue
BGLY46
BSER47
BTHR48
BTYR137
BLYS165
BALA11
BTYR43

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 3PY C 806
ChainResidue
CTYR43
CGLY46
CSER47
CTHR48
CTYR137
CLYS165

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 3PY D 808
ChainResidue
DALA11
DTYR43
DGLY46
DSER47
DTHR48
DTYR137
DLYS165
DTHR167

Functional Information from PROSITE/UniProt
site_idPS00665
Number of Residues18
DetailsDHDPS_1 Dihydrodipicolinate synthase signature 1. GLYvgGSTGEAfvqslsE
ChainResidueDetails
AGLY41-GLU58

site_idPS00666
Number of Residues31
DetailsDHDPS_2 Dihydrodipicolinate synthase signature 2. YNIPalSgvkLtldqintlvtlpg.VgALKQT
ChainResidueDetails
ATYR137-THR167

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:24521460
ChainResidueDetails
AASN138
BASN138
CASN138
DASN138

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Schiff-base intermediate with substrate => ECO:0000269|PubMed:12711733, ECO:0000269|PubMed:19923724, ECO:0000269|PubMed:24521460, ECO:0000269|PubMed:9047371, ECO:0000305|PubMed:8081752
ChainResidueDetails
AGLN166
BGLN166
CGLN166
DGLN166

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:9047371, ECO:0000305|PubMed:12711733, ECO:0007744|PDB:1FDY, ECO:0007744|PDB:1FDZ, ECO:0007744|PDB:1HL2
ChainResidueDetails
ATHR48
AGLY49
BTHR48
BGLY49
CTHR48
CGLY49
DTHR48
DGLY49

site_idSWS_FT_FI4
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL
ChainResidueDetails
ASER168
BTHR209
CSER168
CTYR190
CGLU192
CILE193
CTHR209
DSER168
DTYR190
DGLU192
DILE193
ATYR190
DTHR209
AGLU192
AILE193
ATHR209
BSER168
BTYR190
BGLU192
BILE193

site_idSWS_FT_FI5
Number of Residues8
DetailsSITE: Required to correctly position the proton donor => ECO:0000305|PubMed:24521460
ChainResidueDetails
ATHR48
ATYR111
BTHR48
BTYR111
CTHR48
CTYR111
DTHR48
DTYR111

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 553
ChainResidueDetails
AASN138proton acceptor, proton donor, proton relay
AGLN166covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor

site_idMCSA2
Number of Residues2
DetailsM-CSA 553
ChainResidueDetails
BASN138proton acceptor, proton donor, proton relay
BGLN166covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor

site_idMCSA3
Number of Residues2
DetailsM-CSA 553
ChainResidueDetails
CASN138proton acceptor, proton donor, proton relay
CGLN166covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor

site_idMCSA4
Number of Residues2
DetailsM-CSA 553
ChainResidueDetails
DASN138proton acceptor, proton donor, proton relay
DGLN166covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor

218853

PDB entries from 2024-04-24

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