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4Q2H

Crystal structure of probable proline racemase from agrobacterium radiobacter K84, TARGET EFI-506561, with bound carbonate

Functional Information from GO Data
ChainGOidnamespacecontents
A0016853molecular_functionisomerase activity
A0047580molecular_function4-hydroxyproline epimerase activity
A0050346molecular_functiontrans-L-3-hydroxyproline dehydratase activity
B0016853molecular_functionisomerase activity
B0047580molecular_function4-hydroxyproline epimerase activity
B0050346molecular_functiontrans-L-3-hydroxyproline dehydratase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE BCT A 401
ChainResidue
ASER93
AHOH854
AGLY94
ASER95
AASP251
ACSO255
AGLY256
ATHR257
AHOH850
AHOH851

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 402
ChainResidue
AILE233
AGLY237
ALEU266
APHE278
AHOH535
AHOH608
AHOH733
AHOH742

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BCT B 401
ChainResidue
BSER93
BGLY94
BSER95
BASP251
BCSO255
BGLY256
BTHR257
BHOH818
BHOH819

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"B9JQV3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"B9JQV3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"B9JQV3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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