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2IX9

Respective role of protein folding and glycosylation in the thermal stability of recombinant Feruloyl Esterase A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0005576cellular_componentextracellular region
A0006629biological_processlipid metabolic process
A0016787molecular_functionhydrolase activity
A0016998biological_processcell wall macromolecule catabolic process
A0030245biological_processcellulose catabolic process
A0030248molecular_functioncellulose binding
A0030600molecular_functionferuloyl esterase activity
A0044347biological_processcell wall polysaccharide catabolic process
A0045490biological_processpectin catabolic process
A0045493biological_processxylan catabolic process
A0052689molecular_functioncarboxylic ester hydrolase activity
B0000272biological_processpolysaccharide catabolic process
B0005576cellular_componentextracellular region
B0006629biological_processlipid metabolic process
B0016787molecular_functionhydrolase activity
B0016998biological_processcell wall macromolecule catabolic process
B0030245biological_processcellulose catabolic process
B0030248molecular_functioncellulose binding
B0030600molecular_functionferuloyl esterase activity
B0044347biological_processcell wall polysaccharide catabolic process
B0045490biological_processpectin catabolic process
B0045493biological_processxylan catabolic process
B0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A1267
ChainResidue
AARG162
AALA207
AHIS208
AHOH2281
AHOH2282

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B1265
ChainResidue
BARG162
BALA207
BHIS208
BHOH2243

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CXS A1261
ChainResidue
ATYR25
ATHR68
ASER133
AHIS247
ASER255
AGLY256
AEDO1265
AHOH2271
AHOH2272
AHOH2273
AHOH2274
BASP71

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A1262
ChainResidue
AASP77
ATYR80
AHIS97
ATYR100
ALEU199
AEDO1264

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EDO A1263
ChainResidue
AGLU160
ASER163
AGLY164
APHE168
AALA169
AMET172
ATYR186
AALA207
AGLY209
AHOH2276

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A1264
ChainResidue
AASP77
ATYR100
ASER133
AEDO1262
AHOH2277

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A1265
ChainResidue
ATHR248
ATHR254
ASER255
ACXS1261
AHOH2266
AHOH2278
BGLN45
BASP71

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A1266
ChainResidue
ASER7
AGLU8
AASP9
AHOH2279

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CXS B1261
ChainResidue
AASP71
ALEU74
AHOH2102
BTYR25
BTHR68
BHIS247
BSER255
BGLY256
BHOH2240

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B1262
ChainResidue
BASP77
BTYR80
BHIS97
BTYR100
BEDO1264

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B1263
ChainResidue
BGLU160
BSER163
BGLY164
BPHE168
BTYR186
BALA207
BGLY209
BHOH2241

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B1264
ChainResidue
BLEU74
BASP77
BVAL243
BEDO1262
BHOH2242

Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. LTVTGHSLGA
ChainResidueDetails
ALEU127-ALA136

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:15081808
ChainResidueDetails
ASER133
BSER133

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:15103133
ChainResidueDetails
AASP194
AHIS247
BASP194
BHIS247

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16128806
ChainResidueDetails
AASP77
ATYR80
AHIS247
BASP77
BTYR80
BHIS247

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17027758
ChainResidueDetails
AASN79
BASN79

237735

PDB entries from 2025-06-18

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