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4IMF

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0008747molecular_functionN-acetylneuraminate lyase activity
A0016829molecular_functionlyase activity
A0019262biological_processN-acetylneuraminate catabolic process
B0005737cellular_componentcytoplasm
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 SI3 A 301
ChainResidue
AALA10
AASP190
AGLU191
AILE205
AGLY206
ASER207
ALEU250
ATYR251
AHOH412
AGLY46
ASER47
ATHR48
ATYR136
AILE138
ATHR166
AGLY188
APHE189

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ME2 A 302
ChainResidue
AASP169
ATYR171
AGLU243
AHOH415

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 303
ChainResidue
AGLY168

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 304
ChainResidue
AHIS183

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IPA A 305
ChainResidue
APHE113
AGLN150

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IPA A 306
ChainResidue
APRO158
AVAL160
ALEU161
AASN182

site_idAC7
Number of Residues17
DetailsBINDING SITE FOR RESIDUE SI3 B 301
ChainResidue
BALA10
BGLY46
BSER47
BTHR48
BTYR136
BILE138
BTHR166
BGLY188
BPHE189
BASP190
BGLU191
BILE205
BGLY206
BSER207
BLEU250
BTYR251
BHOH518

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ME2 B 302
ChainResidue
APRO139
APHE140
ALEU141
BPRO139
BPHE140
BLEU141
BGLY143
BHOH527

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ME2 B 303
ChainResidue
BTYR171
BGLU243
BHOH418
BHOH448

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 304
ChainResidue
BTYR180
BPRO181
BASN182
BHIS183

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 2024-08-07

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