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4IMG

Crystal Structure of Pasteurella multocida N-Acetyl-D-Neuraminic acid lyase K164 mutant complexed with N-Glycolylneuraminic acid

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
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE NGF A 501
ChainResidue
AALA10
APHE189
AASP190
AGLU191
AGLY206
ASER207
ALEU250
ATYR251
AHOH833
AGLY46
ASER47
ATHR48
ATYR136
AILE138
APHE140
ATHR166
AGLY188

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ME2 A 502
ChainResidue
ALYS112
APHE140
ALEU141
AGLY143
AHOH779
AHOH790
AHOH892
BLYS112
BPHE140
BGLY143

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ME2 A 503
ChainResidue
ATHR129
AGLY130
ALYS159
AHOH841

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ME2 A 504
ChainResidue
AHIS120
AGLU275
ASER278
AHOH740

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ME2 A 505
ChainResidue
AVAL148
ATYR171
ALEU172
AARG175
AGLU243
AHOH621
AHOH649

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ME2 A 506
ChainResidue
ALEU246
AALA247
ALYS280

site_idAC7
Number of Residues17
DetailsBINDING SITE FOR RESIDUE NGF B 501
ChainResidue
BALA10
BTYR43
BGLY46
BSER47
BTHR48
BTYR136
BILE138
BTHR166
BGLY188
BPHE189
BASP190
BGLU191
BGLY206
BSER207
BLEU250
BTYR251
BHOH799

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ME2 B 502
ChainResidue
BILE146
BGLY147
BVAL148
BTYR171
BGLU243
BHOH663
BHOH926

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ME2 B 503
ChainResidue
BASN248
BSER277
BGLU279
BLYS280
BPHE283

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ME2 B 504
ChainResidue
BASP240
BPHE283
BGLU286
BLEU287
BLYS290
BTYR291
BHOH770

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 Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01237
ChainResidueDetails
ATYR136
BTYR136

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_01237, ECO:0000305|PubMed:24152047
ChainResidueDetails
AALA164
BALA164

site_idSWS_FT_FI3
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:24152047, ECO:0007744|PDB:4IMF
ChainResidueDetails
ASER47
BSER47
BTHR48
BTYR136
BTHR166
BGLY188
BASP190
BGLU191
BSER207
BTYR251
ATHR48
ATYR136
ATHR166
AGLY188
AASP190
AGLU191
ASER207
ATYR251

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PDB entries from 2024-09-11

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