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4J5F

Crystal Structure of B. thuringiensis AiiA mutant F107W

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0102007molecular_functionacyl-L-homoserine-lactone lactonohydrolase activity
A1901335biological_processlactone catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AASP108
AHIS109
AASP191
AHIS235
AZN302
AHOH401

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 302
ChainResidue
AASP191
AZN301
AHOH401
AHIS104
AHIS106
AHIS169

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 303
ChainResidue
ALYS29
ALEU30
AARG89
APHE246
AHOH471

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 304
ChainResidue
AGLU61
ALYS76
AMET77
ATHR78

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 305
ChainResidue
AHIS145
AASN147
ALYS226
AHOH407
AHOH517

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 306
ChainResidue
AALA115
AGLU152
AGLY153
ATYR165
AHOH411
AHOH424

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 307
ChainResidue
AGLU61
AGLY62
AASN65
ALEU74
ATYR249

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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