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

3A93

Crystal structure of hen egg white lysozyme soaked with 30mM RhCl3

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 Residues6
DetailsBINDING SITE FOR RESIDUE NA A 130
ChainResidue
ASER60
ACYS64
ASER72
AARG73
AHOH146
AHOH158

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 131
ChainResidue
ATYR23
AASN113

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 132
ChainResidue
AGLY67
AARG68
ATHR69
AHOH241
AASN65

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 133
ChainResidue
ASER24
AGLY26
AGLN121

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 134
ChainResidue
ALYS33
APHE38

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 135
ChainResidue
AASN65
AHOH162

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE RH3 A 136
ChainResidue
AARG61
AHOH172
AHOH207

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE RH3 A 137
ChainResidue
AARG14
AHIS15
AASP87
ARH3138
ARH3142
AHOH143
AHOH213

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE RH3 A 138
ChainResidue
AASP87
ARH3137
ARH3142
AHOH228

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE RH3 A 139
ChainResidue
AASP18
ARH3141
AHOH234

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE RH3 A 140
ChainResidue
AASP119

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE RH3 A 141
ChainResidue
AASP18
AASN19
ARH3139

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE RH3 A 142
ChainResidue
AARG14
AHIS15
ARH3137
ARH3138
AHOH143

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

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon