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

4DC4

Lysozyme Trimer

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0008152biological_processmetabolic process
A0016231molecular_functionbeta-N-acetylglucosaminidase activity
A0016787molecular_functionhydrolase 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
B0003796molecular_functionlysozyme activity
B0003824molecular_functioncatalytic activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0008152biological_processmetabolic process
B0016231molecular_functionbeta-N-acetylglucosaminidase activity
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016998biological_processcell wall macromolecule catabolic process
B0031640biological_processkilling of cells of another organism
B0042742biological_processdefense response to bacterium
B0042802molecular_functionidentical protein binding
B0050829biological_processdefense response to Gram-negative bacterium
B0050830biological_processdefense response to Gram-positive bacterium
B0051672biological_processobsolete catabolism by organism of cell wall peptidoglycan in other organism
C0003796molecular_functionlysozyme activity
C0003824molecular_functioncatalytic activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005737cellular_componentcytoplasm
C0005783cellular_componentendoplasmic reticulum
C0008152biological_processmetabolic process
C0016231molecular_functionbeta-N-acetylglucosaminidase activity
C0016787molecular_functionhydrolase activity
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0016998biological_processcell wall macromolecule catabolic process
C0031640biological_processkilling of cells of another organism
C0042742biological_processdefense response to bacterium
C0042802molecular_functionidentical protein binding
C0050829biological_processdefense response to Gram-negative bacterium
C0050830biological_processdefense response to Gram-positive bacterium
C0051672biological_processobsolete catabolism by organism of cell wall peptidoglycan in other organism
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 201
ChainResidue
ASER24
AGLY26
AGLN121

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 203
ChainResidue
AASN65
AASP66
AGLY67
ATHR69
ASER72

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 204
ChainResidue
AILE58
AASN59
ATRP63
AALA107
ATRP108
AGLN57

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 205
ChainResidue
AVAL2
BCYS76

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 201
ChainResidue
BGLY71
CASN103
CALA107

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 202
ChainResidue
BSER60
BCYS64
BASN65
BASP66
BSER72

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 203
ChainResidue
BGLU35
BASP52
BGLN57
BILE58
BASN59
BTRP108
BVAL109

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 Residues6
DetailsACT_SITE:
ChainResidueDetails
AGLU35
AASP52
BGLU35
BASP52
CGLU35
CASP52

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AASP101
BASP101
CASP101

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

site_idMCSA2
Number of Residues6
DetailsM-CSA 203
ChainResidueDetails
BGLU35hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BASN46
BASP48
BSER50
BASP52covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
BASN59

site_idMCSA3
Number of Residues6
DetailsM-CSA 203
ChainResidueDetails
CGLU35hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
CASN46
CASP48
CSER50
CASP52covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
CASN59

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon