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8BPH

X-ray structure of the adduct formed upon reaction of Lysozyme with [Ru2Cl(D-p-FPhF)(O2CCH3)3] (Structure 3)

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0003796molecular_functionlysozyme activity
AAA0005515molecular_functionprotein binding
AAA0005576cellular_componentextracellular region
AAA0005615cellular_componentextracellular space
AAA0005737cellular_componentcytoplasm
AAA0005783cellular_componentendoplasmic reticulum
AAA0016231molecular_functionbeta-N-acetylglucosaminidase activity
AAA0016798molecular_functionhydrolase activity, acting on glycosyl bonds
AAA0016998biological_processcell wall macromolecule catabolic process
AAA0031640biological_processkilling of cells of another organism
AAA0042742biological_processdefense response to bacterium
AAA0042802molecular_functionidentical protein binding
AAA0050829biological_processdefense response to Gram-negative bacterium
AAA0050830biological_processdefense response to Gram-positive bacterium
AAA0051672biological_processobsolete catabolism by organism of cell wall peptidoglycan in other organism
Functional Information from PROSITE/UniProt
site_idPS00128
Number of Residues19
DetailsGLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CnipCsaLlssDItasvnC
ChainResidueDetails
AAACYS76-CYS94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AAAGLU35
AAAASP52

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AAAASP101

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 203
ChainResidueDetails
AAAGLU35hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AAAASN46
AAAASP48
AAASER50
AAAASP52covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
AAAASN59

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PDB entries from 2024-11-06

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