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4IME

Crystal Structure of Pasteurella multocida N-Acetyl-D-Neuraminic acid lyase K164A Mutant

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
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0005975biological_processcarbohydrate metabolic process
E0008747molecular_functionN-acetylneuraminate lyase activity
E0016829molecular_functionlyase activity
E0019262biological_processN-acetylneuraminate catabolic process
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0005975biological_processcarbohydrate metabolic process
F0008747molecular_functionN-acetylneuraminate lyase activity
F0016829molecular_functionlyase activity
F0019262biological_processN-acetylneuraminate catabolic process
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0005975biological_processcarbohydrate metabolic process
G0008747molecular_functionN-acetylneuraminate lyase activity
G0016829molecular_functionlyase activity
G0019262biological_processN-acetylneuraminate catabolic process
H0005737cellular_componentcytoplasm
H0005829cellular_componentcytosol
H0005975biological_processcarbohydrate metabolic process
H0008747molecular_functionN-acetylneuraminate lyase activity
H0016829molecular_functionlyase activity
H0019262biological_processN-acetylneuraminate catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ME2 B 301
ChainResidue
ALYS112
APRO139
APHE140
ALEU141
AGLY143
BLYS112
BPHE140
BLEU141
BHOH736

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ME2 B 302
ChainResidue
AASN84
AGLN86
BASP18
BGLY19
BSER20
BSER55
BGLU58
BARG269
BHOH484
BHOH666

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ME2 C 5001
ChainResidue
CLYS112
CPRO139
CPHE140
CLEU141
CGLY143
CHOH5384
DLYS112
DPRO139
DPHE140
DLEU141
DGLY143
DHOH673
DHOH756

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ME2 D 301
ChainResidue
DHOH755
DHOH766
DHOH767
DHOH769
FLYS5
FASP202
FHOH534
FHOH548

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ME2 E 301
ChainResidue
ELYS112
EPHE140
ELEU141
EGLY143
EHOH712
FLYS112
FPRO139
FPHE140
FLEU141
FGLY143

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ME2 E 302
ChainResidue
ELYS93
EHOH446
EHOH617
HASP18
HSER20
HGLU58
HARG269
HHOH395

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ME2 G 301
ChainResidue
GLYS112
GPRO139
GPHE140
GLEU141
GGLY143
GHOH662
HPHE140
HGLY143
HHOH615

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PG6 G 302
ChainResidue
GLEU246
GALA247
GASN248
GLYS280
GHOH571

Functional Information from PROSITE/UniProt
site_idPS00217
Number of Residues26
DetailsSUGAR_TRANSPORT_2 Sugar transport proteins signature 2. VdGLYvGGstgenfmLstEekkeifR
ChainResidueDetails
AVAL39-ARG64

site_idPS00665
Number of Residues18
DetailsDHDPS_1 Dihydrodipicolinate synthase signature 1. GLYvgGSTGENfmlsteE
ChainResidueDetails
AGLY41-GLU58

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01237
ChainResidueDetails
ATYR136
BTYR136
CTYR136
DTYR136
ETYR136
FTYR136
GTYR136
HTYR136

site_idSWS_FT_FI2
Number of Residues8
DetailsACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_01237, ECO:0000305|PubMed:24152047
ChainResidueDetails
AALA164
BALA164
CALA164
DALA164
EALA164
FALA164
GALA164
HALA164

site_idSWS_FT_FI3
Number of Residues72
DetailsBINDING: BINDING => ECO:0000269|PubMed:24152047, ECO:0007744|PDB:4IMF
ChainResidueDetails
ASER47
BSER47
BTHR48
BTYR136
BTHR166
BGLY188
BASP190
BGLU191
BSER207
BTYR251
CSER47
ATHR48
CTHR48
CTYR136
CTHR166
CGLY188
CASP190
CGLU191
CSER207
CTYR251
DSER47
DTHR48
ATYR136
DTYR136
DTHR166
DGLY188
DASP190
DGLU191
DSER207
DTYR251
ESER47
ETHR48
ETYR136
ATHR166
ETHR166
EGLY188
EASP190
EGLU191
ESER207
ETYR251
FSER47
FTHR48
FTYR136
FTHR166
AGLY188
FGLY188
FASP190
FGLU191
FSER207
FTYR251
GSER47
GTHR48
GTYR136
GTHR166
GGLY188
AASP190
GASP190
GGLU191
GSER207
GTYR251
HSER47
HTHR48
HTYR136
HTHR166
HGLY188
HASP190
AGLU191
HGLU191
HSER207
HTYR251
ASER207
ATYR251

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PDB entries from 2024-09-11

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