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5LWO

Structure of Spin-labelled T4 lysozyme mutant L115C-R119C-R1 at 100K

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0009253biological_processpeptidoglycan catabolic process
A0016787molecular_functionhydrolase activity
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 Residues4
Detailsbinding site for residue RXR A 201
ChainResidue
ALYS83
ACYS115
ACYS119
AGLN122

site_idAC2
Number of Residues2
Detailsbinding site for residue CL A 202
ChainResidue
AHIS31
AHOH467

site_idAC3
Number of Residues6
Detailsbinding site for residue CL A 203
ChainResidue
AARG145
AHOH463
AHOH563
ALYS124
ATHR142
AASN144

site_idAC4
Number of Residues11
Detailsbinding site for residue HED A 204
ChainResidue
AASP47
AGLY51
AASN53
ATHR109
AGLY110
AGLY113
APHE114
AHOH323
AHOH344
AHOH424
AHOH439

site_idAC5
Number of Residues3
Detailsbinding site for residue PO4 A 205
ChainResidue
AARG76
AARG80
ALYS85

site_idAC6
Number of Residues3
Detailsbinding site for residue CL A 206
ChainResidue
AASN132
ALYS135
AHOH387

site_idAC7
Number of Residues5
Detailsbinding site for residue CL A 207
ChainResidue
AVAL57
AILE58
AHOH553
AHOH555
AHOH565

site_idAC8
Number of Residues5
Detailsbinding site for residue BME A 208
ChainResidue
AILE3
AASN68
AASP72
AHOH408
AHOH431

site_idAC9
Number of Residues5
Detailsbinding site for residue K A 209
ChainResidue
AGLU11
ATYR18
AHOH358
AHOH393
AHOH528

site_idAD1
Number of Residues5
Detailsbinding site for residue K A 210
ChainResidue
AGLY30
APHE104
AHOH335
AHOH347
AHOH506

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1892846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

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

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PDB entries from 2025-12-24

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