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1FP3

CRYSTAL STRUCTURE OF N-ACYL-D-GLUCOSAMINE 2-EPIMERASE FROM PORCINE KIDNEY

Functional Information from GO Data
ChainGOidnamespacecontents
A0005975biological_processcarbohydrate metabolic process
A0006044biological_processN-acetylglucosamine metabolic process
A0006051biological_processN-acetylmannosamine metabolic process
A0016853molecular_functionisomerase activity
A0019262biological_processN-acetylneuraminate catabolic process
A0030414molecular_functionpeptidase inhibitor activity
A0042802molecular_functionidentical protein binding
A0050121molecular_functionN-acylglucosamine 2-epimerase activity
B0005975biological_processcarbohydrate metabolic process
B0006044biological_processN-acetylglucosamine metabolic process
B0006051biological_processN-acetylmannosamine metabolic process
B0016853molecular_functionisomerase activity
B0019262biological_processN-acetylneuraminate catabolic process
B0030414molecular_functionpeptidase inhibitor activity
B0042802molecular_functionidentical protein binding
B0050121molecular_functionN-acylglucosamine 2-epimerase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues42
DetailsRegion: {"description":"Leucine-zipper"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsSite: {"description":"Important for enzyme activity","evidences":[{"source":"UniProtKB","id":"P51606","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242500

PDB entries from 2025-10-01

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