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4KEQ

Crystal structure of 4-pyridoxolactonase, 5-pyridoxolactone bound

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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AASP100
AHIS101
AASP207
AHIS252
AHOH401

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 302
ChainResidue
AHOH401
AHIS96
AHIS98
AHIS185
AASP207

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 5PN A 303
ChainResidue
AGLU65
AHIS98
APHE99
ALEU132
AGLY133
ATYR210
APHE223
AHOH401

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 5PN A 304
ChainResidue
AASP10
ASER13
AILE68
AGLU70
AGLN73
AMET254
ALYS258

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 305
ChainResidue
ACYS115
AHIS116
AARG117
AVAL120
AGLY166

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 306
ChainResidue
AGLU142
AARG159
AARG199
AARG261
AGLY268
AHIS269
AHIS271

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 307
ChainResidue
AVAL31
AARG32
APHE33
ATHR211
AHIS252
AASP253
AMET254

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 308
ChainResidue
AASP54
ALYS106
AASP136
ASER138

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 309
ChainResidue
AARG32
AMET254

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 310
ChainResidue
AASN125
APRO126
AGLN127
APRO128

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255
ChainResidueDetails
AASP100

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:24699732
ChainResidueDetails
AHIS96
AHIS98
AASP100
AHIS101
AHIS185
AASP207
AHIS252

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PDB entries from 2024-04-24

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