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

3WL2

Monoclinic Lysozyme at 0.96 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0016231molecular_functionbeta-N-acetylglucosaminidase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0042802molecular_functionidentical protein binding
A0050829biological_processdefense response to Gram-negative bacterium
A0050830biological_processdefense response to Gram-positive bacterium
A0051672biological_processobsolete catabolism by organism of cell wall peptidoglycan in other organism
B0003796molecular_functionlysozyme activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0016231molecular_functionbeta-N-acetylglucosaminidase 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
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 A 201
ChainResidue
AASP66
APRO79
ACYS80
ASER81
AHOH324
BARG21
BGLY22
BHOH391

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 A 202
ChainResidue
AASN74
AASN77
AILE78
APRO79
BARG112
BLYS116
AASN65

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NO3 A 203
ChainResidue
AGLY126
AARG128

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 204
ChainResidue
APHE3
AARG14
AHIS15
AASP87
AILE88
AHOH413

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO3 A 205
ChainResidue
AARG5
ALYS33
APHE38
ATRP123
AHOH357

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO3 A 206
ChainResidue
ASER24
ALEU25
AGLY26
AGLN121
AILE124

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 A 207
ChainResidue
ALYS116
AHOH432
BASN65
BASN74
BASN77
BILE78
BPRO79
BHOH448

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 208
ChainResidue
ATYR20
AARG21
AALA110
AASN113
AARG114
AHOH321

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 209
ChainResidue
AARG21
AHOH401
AHOH448

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 210
ChainResidue
AGLN57
AASN59
ATRP63
AALA107
ATRP108
AHOH407
AHOH449

site_idBC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE NO3 B 201
ChainResidue
BHIS15
BGLY16
BTYR20
BLYS96
BALA110
BASN113
BARG114
BNA203
BHOH352
BHOH405

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO3 B 202
ChainResidue
BTRP63
BALA107
BHOH321
BHOH453
BHOH454

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 203
ChainResidue
BPHE34
BARG114
BNO3201
BHOH482

Functional Information from PROSITE/UniProt
site_idPS00128
Number of Residues19
DetailsGLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CnipCsaLlssDItasvnC
ChainResidueDetails
ACYS76-CYS94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE:
ChainResidueDetails
AGLU35
AASP52
BGLU35
BASP52

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AASP101
BASP101

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 203
ChainResidueDetails
AGLU35hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AASN46
AASP48
ASER50
AASP52covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
AASN59

site_idMCSA2
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

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon