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

217L

STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0008152biological_processmetabolic process
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 CL A 178
ChainResidue
AHIS31
ALYS135
AHOH182
AHOH220

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME A 900
ChainResidue
AASN144
AARG148
AHOH230

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BME A 901
ChainResidue
AVAL75
ABME902

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME A 902
ChainResidue
ATYR88
AALA93
AILE100
AHOH195
ABME901

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

218196

PDB entries from 2024-04-10

PDB statisticsPDBj update infoContact PDBjnumon