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5EHT

Indirect contributions of mutations underlie optimization of new enzyme function

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
AHOH432

site_idAC2
Number of Residues6
Detailsbinding site for residue ZN A 302
ChainResidue
AASP191
AZN301
AHOH432
AHIS104
AHIS106
AHIS169

site_idAC3
Number of Residues8
Detailsbinding site for residue GOL A 303
ChainResidue
AASN59
AASN60
AGLU61
ALYS76
AMET77
AHOH433
AHOH449
AHOH506

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 304
ChainResidue
AHIS106
AARG134
AGLU136
AHIS169
AGLY207
APHE208
AHOH576

site_idAC5
Number of Residues5
Detailsbinding site for residue GOL A 305
ChainResidue
ALEU30
AARG89
APHE246
AHOH423
AHOH436

site_idAC6
Number of Residues5
Detailsbinding site for residue GOL A 306
ChainResidue
APRO94
AALA115
AGLU152
AHOH414
AHOH462

site_idAC7
Number of Residues10
Detailsbinding site for residue GOL A 307
ChainResidue
AMET53
AGLU55
AILE83
AGLY111
AALA115
AGLU152
AHOH426
AHOH445
AHOH448
AHOH556

site_idAC8
Number of Residues8
Detailsbinding site for residue GOL A 308
ChainResidue
AHIS145
ALEU146
AASN147
AGLU222
ALYS226
AHOH417
AHOH439
AHOH534

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS104
AHIS106
AASP108
AHIS109
AHIS169
AASP191
AHIS235

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PDB entries from 2024-11-06

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