Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8URO

Crystal structure of IgG1-Fc fragment (E382S) in complex with Corynebacterial ENGase CU43 (D187A-E189A)

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0006508biological_processproteolysis
D0008233molecular_functionpeptidase activity
D0016787molecular_functionhydrolase activity
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. FSCSVMH
ChainResidueDetails
BPHE423-HIS429

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues99
DetailsDomain: {"description":"Ig-like 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"19358553","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29449492","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

254917

PDB entries from 2026-06-10

PDB statisticsPDBj update infoContact PDBjnumon