Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2OU8

Structure of Spin-labeled T4 Lysozyme Mutant T115R1 at Room Temperature

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0009253biological_processpeptidoglycan catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
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 Residues9
DetailsBINDING SITE FOR RESIDUE MTN A 165
ChainResidue
ASER38
AASN40
AALA41
ALYS83
AVAL87
AALA112
ACYS115
AASN116
AARG119

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BME A 181
ChainResidue
AHOH223
AHOH264

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BME A 183
ChainResidue
AASP20
ATHR26
AGLY30
ALEU32
APHE104
AHOH241
AHOH251

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME A 185
ChainResidue
APHE4
AGLU5
AHOH267

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME A 187
ChainResidue
AMET106
AARG137
AHOH224

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_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 206l
ChainResidueDetails
AGLU11
AASP20

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

221371

PDB entries from 2024-06-19

PDB statisticsPDBj update infoContact PDBjnumon