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3RU5

Silver Metallated Hen Egg White Lysozyme at 1.35 A

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 Residues5
DetailsBINDING SITE FOR RESIDUE AG A 300
ChainResidue
AARG14
AHIS15
AASP87
ATHR89
ANO3301

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NO3 A 301
ChainResidue
ASER86
AASP87
AILE88
AHOH204
AAG300
APHE3
AALA11
AARG14
AHIS15

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NO3 A 132
ChainResidue
ACYS64
AASN65
AASP66
AGLY67
AARG68
ATHR69
ASER72
ANA133
AHOH152

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 133
ChainResidue
ASER60
ACYS64
ASER72
AARG73
ANO3132
AHOH152

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 134
ChainResidue
ATYR53
AGLY54
AILE55
ALEU56
AGLN57
ASER91

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 135
ChainResidue
AGLN41
AALA42
ATHR43
ATYR53
AARG68

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA A 136
ChainResidue
AARG45
AGLY49
ASER50
ATHR51
AASP66
AARG68
ATHR69

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 137
ChainResidue
ATRP111
AARG114
AHOH153
AHOH172

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 138
ChainResidue
AARG21
AVAL99
ASER100
AGLY102
AASN103
AGLY104
AVAL109
AASN113
AHOH154

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NO3 A 139
ChainResidue
AARG5
ALYS33
APHE38
ATRP123

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 140
ChainResidue
ASER24
ALEU25
AGLY26
AGLN121
AILE124
AHOH201

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 141
ChainResidue
AGLN57
AILE58
AASN59
ATRP63
AALA107
ATRP108

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 A 142
ChainResidue
ASER24
AASN27
AARG114
AVAL120
AHOH144
AHOH161
AHOH172
AHOH201

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO3 A 143
ChainResidue
AASN65
AASN74
AASN77
AILE78
APRO79

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

225946

PDB entries from 2024-10-09

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