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1PQK

Repacking of the Core of T4 Lysozyme by Automated Design

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
B0003796molecular_functionlysozyme activity
B0009253biological_processpeptidoglycan catabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016998biological_processcell wall macromolecule catabolic process
B0030430cellular_componenthost cell cytoplasm
B0031640biological_processkilling of cells of another organism
B0042742biological_processdefense response to bacterium
B0044659biological_processviral release from host cell by cytolysis
C0003796molecular_functionlysozyme activity
C0009253biological_processpeptidoglycan catabolic process
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0016998biological_processcell wall macromolecule catabolic process
C0030430cellular_componenthost cell cytoplasm
C0031640biological_processkilling of cells of another organism
C0042742biological_processdefense response to bacterium
C0044659biological_processviral release from host cell by cytolysis
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
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
BGLU11
CGLU11

site_idSWS_FT_FI2
Number of Residues3
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
BASP20
CASP20

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU32
APHE104
BLEU32
BPHE104
CLEU32
CPHE104

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER117
AASN132
BSER117
BASN132
CSER117
CASN132

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

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 206l
ChainResidueDetails
BGLU11
BASP20

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 206l
ChainResidueDetails
CGLU11
CASP20

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

site_idMCSA2
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
BGLU11proton shuttle (general acid/base)
BASP20covalent catalysis

site_idMCSA3
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
CGLU11proton shuttle (general acid/base)
CASP20covalent catalysis

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PDB entries from 2024-07-10

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