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4J9X

Crystal structure of the complex of a hydroxyproline epimerase (TARGET EFI-506499, PSEUDOMONAS FLUORESCENS PF-5) with trans-4-hydroxy-l-proline

Functional Information from GO Data
ChainGOidnamespacecontents
A0016853molecular_functionisomerase activity
A0047580molecular_function4-hydroxyproline epimerase activity
B0016853molecular_functionisomerase activity
B0047580molecular_function4-hydroxyproline epimerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HYP A 401
ChainResidue
ALEU85
ATHR238
AHOH516
ACYS88
AGLY89
AHIS90
AHIS208
ACYS226
AASP232
ACYS236
AGLY237

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 402
ChainResidue
AASP215
AALA218
AHOH581
AHOH777
AHOH825
AHOH826

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HYP B 401
ChainResidue
BLEU85
BCYS88
BGLY89
BHIS90
BHIS208
BCYS226
BASP232
BCYS236
BGLY237
BTHR238
BHOH513

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 402
ChainResidue
BASP215
BALA218
BHOH565
BHOH690
BHOH699
BHOH713

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:24980702
ChainResidueDetails
ACYS88
BCYS88

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:24980702
ChainResidueDetails
ACYS236
BCYS236

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:24980702
ChainResidueDetails
AGLY89
AHIS208
AASP232
AGLY237
BGLY89
BHIS208
BASP232
BGLY237

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PDB entries from 2024-11-13

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