Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2NTP

Crystal structure of pectin methylesterase in complex with hexasaccharide VI

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0009279cellular_componentcell outer membrane
A0009405biological_processobsolete pathogenesis
A0016787molecular_functionhydrolase activity
A0030599molecular_functionpectinesterase activity
A0042545biological_processcell wall modification
A0045490biological_processpectin catabolic process
A0052689molecular_functioncarboxylic ester hydrolase activity
A0071555biological_processcell wall organization
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0009279cellular_componentcell outer membrane
B0009405biological_processobsolete pathogenesis
B0016787molecular_functionhydrolase activity
B0030599molecular_functionpectinesterase activity
B0042545biological_processcell wall modification
B0045490biological_processpectin catabolic process
B0052689molecular_functioncarboxylic ester hydrolase activity
B0071555biological_processcell wall organization
Functional Information from PROSITE/UniProt
site_idPS00503
Number of Residues10
DetailsPECTINESTERASE_2 Pectinesterase signature 2. IsGTVDFIFG
ChainResidueDetails
AILE194-GLY203

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:17717531
ChainResidueDetails
AASP178
BASP178

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:17717531
ChainResidueDetails
AASP199
BASP199

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:17717531
ChainResidueDetails
ATHR109
BGLN153
BARG219
BASN226
BTYR230
BARG267
BTRP269
BTHR272
AGLN153
AARG219
AASN226
ATYR230
AARG267
ATRP269
ATHR272
BTHR109

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000269|PubMed:17717531
ChainResidueDetails
AGLN177
BGLN177

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1gq8
ChainResidueDetails
AASP199
AGLN177
AASP178
AGLN153

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1gq8
ChainResidueDetails
BASP199
BGLN177
BASP178
BGLN153

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon