Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4LFP

X-ray structure of the adduct between hen egg white lysozyme and a homoleptic gold(I) complex with the saccharynate ligand

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0016231molecular_functionbeta-N-acetylglucosaminidase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0042802molecular_functionidentical protein binding
A0050829biological_processdefense response to Gram-negative bacterium
A0050830biological_processdefense response to Gram-positive bacterium
A0051672biological_processobsolete catabolism by organism of cell wall peptidoglycan in other organism
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE AU A 301
ChainResidue
AARG14
AHIS15
AILE88
ACL302

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 302
ChainResidue
AASP87
AILE88
AAU301
AHOH448

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 303
ChainResidue
AALA110
AASN113
ATYR23

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 304
ChainResidue
AASN65
AGLY67
AARG68
ATHR69
AHOH447

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 305
ChainResidue
ASER60
ACYS64
ASER72
AARG73
AHOH414
AHOH419

Functional Information from PROSITE/UniProt
site_idPS00128
Number of Residues19
DetailsGLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CnipCsaLlssDItasvnC
ChainResidueDetails
ACYS76-CYS94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AGLU35
AASP52

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AASP101

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 203
ChainResidueDetails
AGLU35hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AASN46
AASP48
ASER50
AASP52covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
AASN59

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon