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1C68

T4 LYSOZYME MUTANT C54T/C97A/L121A/L133A IN THE PRESENCE OF 8 ATM XENON

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0009253biological_processpeptidoglycan catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 173
ChainResidue
ATHR142
AARG145
AHOH214
AHOH291

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 178
ChainResidue
AALA49
ALYS135
AHOH215

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE XE A 500
ChainResidue
AXE501
AXE502
AALA133
APHE153

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE XE A 501
ChainResidue
ALEU118
AXE500

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE XE A 502
ChainResidue
APHE153
AARG154
AXE500

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME A 901
ChainResidue
AVAL71
AASP72
ABME902
ABME902

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME A 902
ChainResidue
AILE3
AASP72
AHOH195
ABME901
ABME901

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AGLU11

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AASP20

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU32
APHE104

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER117
AASN132

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 206l
ChainResidueDetails
AGLU11
AASP20

site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU11proton shuttle (general acid/base)
AASP20covalent catalysis

222036

PDB entries from 2024-07-03

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