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2Z6B

Crystal Structure Analysis of (gp27-gp5)3 conjugated with Fe(III) protoporphyrin

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0005515molecular_functionprotein binding
A0009253biological_processpeptidoglycan catabolic process
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
A0044409biological_processsymbiont entry into host
A0046718biological_processsymbiont entry into host cell
A0098003biological_processviral tail assembly
A0098015cellular_componentvirus tail
A0098025cellular_componentvirus tail, baseplate
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
D0005515molecular_functionprotein binding
D0098003biological_processviral tail assembly
D0098015cellular_componentvirus tail
D0098025cellular_componentvirus tail, baseplate
Functional Information from PROSITE/UniProt
site_idPS00066
Number of Residues15
DetailsHMG_COA_REDUCTASE_1 Hydroxymethylglutaryl-coenzyme A reductases signature 1. KfVFvWQDiMGvNmM
ChainResidueDetails
DLYS184-MET198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_04151, ECO:0000305|PubMed:11823865
ChainResidueDetails
AGLU184

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_04151, ECO:0000305|PubMed:11823865
ChainResidueDetails
AASP193

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Cleavage => ECO:0000255|HAMAP-Rule:MF_04151, ECO:0000269|PubMed:10217762, ECO:0000269|PubMed:15701513
ChainResidueDetails
ALEU351

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 206l
ChainResidueDetails
AASP193
AGLU184

222415

PDB entries from 2024-07-10

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