Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5JEN

Crystal structure of the anti-sigma factor RsiV bound to lysozyme

Functional Information from GO Data
ChainGOidnamespacecontents
B0003796molecular_functionlysozyme activity
B0003824molecular_functioncatalytic activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0016231molecular_functionbeta-N-acetylglucosaminidase activity
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016998biological_processcell wall macromolecule catabolic process
B0031640biological_processkilling of cells of another organism
B0042742biological_processdefense response to bacterium
B0042802molecular_functionidentical protein binding
B0050829biological_processdefense response to Gram-negative bacterium
B0050830biological_processdefense response to Gram-positive bacterium
B0051672biological_processobsolete catabolism by organism of cell wall peptidoglycan in other organism
D0003796molecular_functionlysozyme activity
D0003824molecular_functioncatalytic activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005737cellular_componentcytoplasm
D0005783cellular_componentendoplasmic reticulum
D0016231molecular_functionbeta-N-acetylglucosaminidase activity
D0016787molecular_functionhydrolase activity
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0016998biological_processcell wall macromolecule catabolic process
D0031640biological_processkilling of cells of another organism
D0042742biological_processdefense response to bacterium
D0042802molecular_functionidentical protein binding
D0050829biological_processdefense response to Gram-negative bacterium
D0050830biological_processdefense response to Gram-positive bacterium
D0051672biological_processobsolete catabolism by organism of cell wall peptidoglycan in other organism
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue NA A 400
ChainResidue
ATHR239
AHOH506
AHOH538
AHOH571
AHOH584
AHOH607

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 401
ChainResidue
AHOH504
BASP52
BHOH311
ASER168
ASER169
ATYR255

site_idAC3
Number of Residues7
Detailsbinding site for residue NA B 200
ChainResidue
BSER60
BCYS64
BASN65
BSER72
BARG73
BHOH318
BHOH341

site_idAC4
Number of Residues4
Detailsbinding site for residue CL B 201
ChainResidue
ALYS232
BGLY67
BARG68
BTHR69

site_idAC5
Number of Residues6
Detailsbinding site for residue NA C 400
ChainResidue
CTHR239
CHOH545
CHOH583
CHOH586
CHOH613
CHOH615

site_idAC6
Number of Residues6
Detailsbinding site for residue NA C 401
ChainResidue
CSER168
CSER169
CTYR255
CHOH507
DASP52
DHOH336

site_idAC7
Number of Residues6
Detailsbinding site for residue NA D 200
ChainResidue
DSER60
DCYS64
DSER72
DARG73
DHOH337
DHOH344

site_idAC8
Number of Residues6
Detailsbinding site for residue CL D 201
ChainResidue
CLYS232
DASN65
DGLY67
DARG68
DTHR69
DSER72

Functional Information from PROSITE/UniProt
site_idPS00128
Number of Residues19
DetailsGLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CnipCsaLlssDItasvnC
ChainResidueDetails
BCYS76-CYS94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues256
DetailsDomain: {"description":"C-type lysozyme","evidences":[{"source":"PROSITE-ProRule","id":"PRU00680","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 203
ChainResidueDetails
BGLU35hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BASN46
BASP48
BSER50
BASP52covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
BASN59

site_idMCSA2
Number of Residues6
DetailsM-CSA 203
ChainResidueDetails
DGLU35hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
DASN46
DASP48
DSER50
DASP52covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
DASN59

240971

PDB entries from 2025-08-27

PDB statisticsPDBj update infoContact PDBjnumon