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2D4I

Monoclinic hen egg-white lysozyme crystallized at pH4.5 form heavy water solution

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
B0003796molecular_functionlysozyme activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0016231molecular_functionbeta-N-acetylglucosaminidase 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
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 A 401
ChainResidue
AASN65
AASN74
AASN77
AILE78
APRO79
ADOD545
ADOD596
BLYS316

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 B 402
ChainResidue
ALYS116
BASN265
BASN274
BASN277
BILE278
BPRO279
AARG112

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 B 403
ChainResidue
AARG21
AGLY22
BASN265
BASP266
BARG268
BCYS280
BSER281

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NO3 B 404
ChainResidue
BGLY326

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE NO3 B 405
ChainResidue
BSER260
BCYS264
BASN265
BASP266
BGLY267
BARG268
BTHR269
BSER272
BARG273
BNA406

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA B 406
ChainResidue
BSER260
BCYS264
BSER272
BARG273
BNO3405
BDOD407
BDOD409

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 Residues4
DetailsACT_SITE:
ChainResidueDetails
AGLU35
AASP52
BGLU235
BASP252

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AASP101
BASP301

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 132l
ChainResidueDetails
AGLU35
AASP52

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 132l
ChainResidueDetails
BGLU235
BASP252

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
BGLU235hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BASN246
BASP248
BSER250
BASP252covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
BASN259

222926

PDB entries from 2024-07-24

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