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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
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 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
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

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PDB entries from 2024-07-31

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