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5YFE

Enzymatic and structural characterization of the poly (ethylene terephthalate) hydrolase PETase from I. sakaiensis

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue SO4 A 301
ChainResidue
AGLN93
APRO94
ASER95
AHOH412

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 302
ChainResidue
ATYR193
AASN261
AHOH435

site_idAC3
Number of Residues9
Detailsbinding site for residue GOL A 303
ChainResidue
ASER166
ASER167
ASER264
ALEU265
AGLU266
AHIS267
AGOL304
AASN164
APHE165

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 304
ChainResidue
APHE235
AASN262
ACYS263
ASER264
AGOL303
AHOH403
AHOH429

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
ASER134

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
AASP180
AHIS211

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:29235460
ChainResidueDetails
ATYR61
AMET135

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:29235460, ECO:0000305|PubMed:29666242
ChainResidueDetails
ATRP159

237735

PDB entries from 2025-06-18

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