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5JGZ

Spin-Labeled T4 Lysozyme Construct T151V1

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 Residues3
Detailsbinding site for residue CL A 201
ChainResidue
AASN132
ALYS135
AHOH380

site_idAC2
Number of Residues6
Detailsbinding site for residue K A 202
ChainResidue
AGLU11
ATYR18
AHOH338
AHOH393
AHOH418
AHOH494

site_idAC3
Number of Residues4
Detailsbinding site for residue V1A A 203
ChainResidue
ALYS147
ACYS151
AARG154
AHOH493

site_idAC4
Number of Residues8
Detailsbinding site for residue PO4 A 204
ChainResidue
ALYS19
AARG125
ATRP126
AASP127
AGLU128
AHOH308
AHOH335
AHOH453

site_idAC5
Number of Residues7
Detailsbinding site for residue HEZ A 205
ChainResidue
AGLU22
ATYR24
AILE50
AGLY51
AARG52
AARG137
AHOH323

site_idAC6
Number of Residues7
Detailsbinding site for residue HEZ A 206
ChainResidue
AGLY30
ALEU32
AVAL103
AGLU108
AHOH317
AHOH340
AHOH388

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_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU11proton shuttle (general acid/base)
AASP20covalent catalysis

224572

PDB entries from 2024-09-04

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