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4KEP

Crystal structure of 4-pyridoxolactonase, wild-type

Replaces:  3AJ0
Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0042820biological_processvitamin B6 catabolic process
A0046872molecular_functionmetal ion binding
A0047585molecular_function4-pyridoxolactonase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AASP100
AHIS101
AASP207
AHIS252
AZN302
AACT303

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 302
ChainResidue
AASP207
AZN301
AACT303
AHIS96
AHIS98
AHIS185

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ACT A 303
ChainResidue
AHIS96
AHIS98
AASP100
AHIS101
AHIS185
AASP207
ATYR210
AHIS252
AZN301
AZN302
AEDO307

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 304
ChainResidue
AVAL21
AVAL31
AARG32
AHIS252
AASP253
AMET254

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 305
ChainResidue
AVAL120

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 306
ChainResidue
ALYS66
AARG117
ASER118

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 307
ChainResidue
APHE33
AGLU65
APHE99
APHE223
AACT303

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 308
ChainResidue
AILE68
AGLU70
AGLU165
AGLY166
AILE167
AHIS273
AHOH438
AHOH439
AHOH447
AHOH451
AHOH473

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 309
ChainResidue
AARG261
AGLY268
AHIS269

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24699732","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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