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4ARJ

Crystal structure of a pesticin (translocation and receptor binding domain) from Y. pestis and T4-lysozyme chimera

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1336
ChainResidue
AILE176
AASP177
AGLU178
AGLY179
ALYS250
ATHR282

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1337
ChainResidue
AASN311
AARG312
AHOH2007
ALYS250
ATHR309
APRO310

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 1336
ChainResidue
BLYS250
BTHR309
BPRO310
BASN311
BARG312

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1337
ChainResidue
BILE176
BASP177
BLYS250

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1338
ChainResidue
ALYS215
BARG286
BARG292

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AGLU178
BGLU178

site_idSWS_FT_FI2
Number of Residues2
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
AASP187
BASP187

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU199
APHE271
BLEU199
BPHE271

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER284
AASN299
BSER284
BASN299

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU178proton shuttle (general acid/base)
AASP187covalent catalysis

site_idMCSA2
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
BGLU178proton shuttle (general acid/base)
BASP187covalent catalysis

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PDB entries from 2024-07-31

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