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3DHA

An Ultral High Resolution Structure of N-Acyl Homoserine Lactone Hydrolase with the Product N-Hexanoyl-L-Homoserine Bound at An Alternative Site

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0102007molecular_functionacyl-L-homoserine-lactone lactonohydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 255
ChainResidue
AASP112
AHIS113
AASP195
AHIS239
AHOH307

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 256
ChainResidue
AHOH307
AHIS108
AHIS110
AHIS173
AASP195

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE C6L A 257
ChainResidue
ASER24
APHE72
AGLN76
AILE77
AHIS110
APHE111
AGLU140
ATYR198
AHOH290
AHOH300
AHOH326
AHOH447
AHOH466

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 258
ChainResidue
ALEU34
AARG93
APHE250
AHOH344
AHOH394

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 259
ChainResidue
APRO98
AALA119
ATHR130
AGLY157
ATYR169
AHOH264
AHOH306
AHOH389
AHOH513

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 260
ChainResidue
AMET57
AGLU59
AILE87
AGLY115
AALA119
AGLU156
AHOH270
AHOH316
AHOH348
AHOH357
AHOH433

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 261
ChainResidue
AHIS149
ALEU150
AASN151
ALYS230
AHOH304
AHOH327
AHOH342
AHOH482

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING:
ChainResidueDetails
AHIS108
AHIS110
AASP112
AHIS113
AHIS173
AASP195
AHIS239

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
AASP112
AASN202

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 2bmi
ChainResidueDetails
AASP112

237735

PDB entries from 2025-06-18

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