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

3GUO

T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--phenol binding

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 Residues7
DetailsBINDING SITE FOR RESIDUE IPH A 501
ChainResidue
AALA99
AGLU102
AVAL103
AVAL111
ALEU121
APHE153
AHOH601

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 165
ChainResidue
AASP144
AARG145
ACYS142
APRO143

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA A 166
ChainResidue
ATYR88
BTYR88

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IPH B 501
ChainResidue
BALA99
BGLU102
BVAL111
BLEU121
BPHE153
BHOH602

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 165
ChainResidue
BCYS142
BPRO143
BASP144
BARG145

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
AGLU11
BGLU11

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
AASP20
BASP20

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU32
APHE104
BLEU32
BPHE104

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
AVAL117
AASN132
BVAL117
BASN132

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 206l
ChainResidueDetails
AGLU11
AASP20

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 206l
ChainResidueDetails
BGLU11
BASP20

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

site_idMCSA2
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
BGLU11proton shuttle (general acid/base)
BASP20covalent catalysis

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon