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3RNX

Crystal Structure of Lysozyme in 30% ethanol

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EOH A 130
ChainResidue
AASN19
AGLY22
APHE34
AHOH212

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EOH A 132
ChainResidue
ATRP62
AASP101
AEOH137

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EOH A 133
ChainResidue
ACYS6
AGLU7
AGLY4
AARG5

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EOH A 134
ChainResidue
AILE58
AASN59
ATRP63
AALA107
AEOH137

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EOH A 135
ChainResidue
AALA82
ASER85
AASP87
ATHR89
AALA90

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EOH A 136
ChainResidue
AASN65
ASER72
AARG73
AASN74
ANA148
AHOH181

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EOH A 137
ChainResidue
ATRP63
AEOH132
AEOH134

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 138
ChainResidue
ASER24
AGLY26
AGLN121

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CL A 139
ChainResidue
AASN65
AGLY67
AARG68
ATHR69
ASER72
AHOH159
AHOH186

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CL A 140
ChainResidue
AGLY49
ASER50
ATHR51
ASER60
AASP66
AARG68
ATHR69

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 142
ChainResidue
AARG73
AASN74

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 143
ChainResidue
AASN65
APRO79

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 144
ChainResidue
ALYS1
AASN39
AGLN41
AASP66
AHOH150

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 145
ChainResidue
AGLN41
ATHR43
ATYR53
AARG68

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 146
ChainResidue
ATYR23
AASN113

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 147
ChainResidue
AHIS15
AASN93
ALYS96

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 148
ChainResidue
ASER60
ACYS64
ASER72
AARG73
AEOH136
AHOH159

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

218853

PDB entries from 2024-04-24

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