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5XFY

Crystal structure of a novel PET hydrolase S131A mutant from Ideonella sakaiensis 201-F6

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0008126molecular_functionacetylesterase activity
A0016787molecular_functionhydrolase activity
A0042178biological_processxenobiotic catabolic process
A0052689molecular_functioncarboxylic ester hydrolase activity
A0071310biological_processcellular response to organic substance
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue SO4 A 301
ChainResidue
AGLY57
ATYR58
AARG103
AALA131
AMET132
AHIS208
AGOL304
AHOH452

site_idAC2
Number of Residues8
Detailsbinding site for residue SO4 A 302
ChainResidue
ATHR22
AASP157
ASER159
AASN161
APHE162
AHOH407
AHOH410
AGLY19

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 303
ChainResidue
ATYR3
ALYS148
AASN235

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 304
ChainResidue
ATYR58
ASER96
AALA100
ASO4301
AHOH404

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:29235460, ECO:0000305|PubMed:29374183, ECO:0000305|PubMed:29603535, ECO:0000305|PubMed:29666242
ChainResidueDetails
AALA131

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:29235460, ECO:0000305|PubMed:29374183, ECO:0000305|PubMed:29603535, ECO:0000305|PubMed:29666242
ChainResidueDetails
AASP177
AHIS208

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:29235460
ChainResidueDetails
AMET132
ATYR58

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:29235460, ECO:0000305|PubMed:29666242
ChainResidueDetails
ATRP156

220472

PDB entries from 2024-05-29

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