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3CSQ

Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044423cellular_componentvirion component
A0046718biological_processsymbiont entry into host cell
A0046872molecular_functionmetal ion binding
A0071555biological_processcell wall organization
A0098003biological_processviral tail assembly
A0098004biological_processvirus tail fiber assembly
A0098023cellular_componentvirus tail, tip
A0098932biological_processsymbiont entry into host cell via disruption of host cell wall peptidoglycan
A0098994biological_processsymbiont entry into host cell via disruption of host cell envelope
A0099002biological_processsymbiont genome ejection through host cell envelope, short tail mechanism
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0031640biological_processkilling of cells of another organism
B0042742biological_processdefense response to bacterium
B0044423cellular_componentvirion component
B0046718biological_processsymbiont entry into host cell
B0046872molecular_functionmetal ion binding
B0071555biological_processcell wall organization
B0098003biological_processviral tail assembly
B0098004biological_processvirus tail fiber assembly
B0098023cellular_componentvirus tail, tip
B0098932biological_processsymbiont entry into host cell via disruption of host cell wall peptidoglycan
B0098994biological_processsymbiont entry into host cell via disruption of host cell envelope
B0099002biological_processsymbiont genome ejection through host cell envelope, short tail mechanism
C0006508biological_processproteolysis
C0008237molecular_functionmetallopeptidase activity
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0031640biological_processkilling of cells of another organism
C0042742biological_processdefense response to bacterium
C0044423cellular_componentvirion component
C0046718biological_processsymbiont entry into host cell
C0046872molecular_functionmetal ion binding
C0071555biological_processcell wall organization
C0098003biological_processviral tail assembly
C0098004biological_processvirus tail fiber assembly
C0098023cellular_componentvirus tail, tip
C0098932biological_processsymbiont entry into host cell via disruption of host cell wall peptidoglycan
C0098994biological_processsymbiont entry into host cell via disruption of host cell envelope
C0099002biological_processsymbiont genome ejection through host cell envelope, short tail mechanism
D0006508biological_processproteolysis
D0008237molecular_functionmetallopeptidase activity
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0031640biological_processkilling of cells of another organism
D0042742biological_processdefense response to bacterium
D0044423cellular_componentvirion component
D0046718biological_processsymbiont entry into host cell
D0046872molecular_functionmetal ion binding
D0071555biological_processcell wall organization
D0098003biological_processviral tail assembly
D0098004biological_processvirus tail fiber assembly
D0098023cellular_componentvirus tail, tip
D0098932biological_processsymbiont entry into host cell via disruption of host cell wall peptidoglycan
D0098994biological_processsymbiont entry into host cell via disruption of host cell envelope
D0099002biological_processsymbiont genome ejection through host cell envelope, short tail mechanism
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 335
ChainResidue
DHIS188
DASP195
DHIS280
DHOH371

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 335
ChainResidue
CHIS188
CASP195
CHIS280
CHOH355

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 335
ChainResidue
BASP195
BHIS280
BHOH376
BHIS188

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 335
ChainResidue
AHIS188
AASP195
AHIS280
AHOH359

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: For lysozyme-like glycosidase activity => ECO:0000305
ChainResidueDetails
AGLU45
BGLU45
CGLU45
DGLU45

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0007744|PDB:3CSZ, ECO:0007744|PDB:3CT0, ECO:0007744|PDB:3CT1, ECO:0007744|PDB:3CT5
ChainResidueDetails
DGLU45
DTHR71
DGLN106
DGLU137
AGLU45
ATHR71
AGLN106
AGLU137
BGLU45
BTHR71
BGLN106
BGLU137
CGLU45
CTHR71
CGLN106
CGLU137

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0007744|PDB:3CSQ
ChainResidueDetails
AHIS188
AASP195
AHIS280
BHIS188
BASP195
BHIS280
CHIS188
CASP195
CHIS280
DHIS188
DASP195
DHIS280

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PDB entries from 2024-06-12

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