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

2F4A

Triclinic cross-linked lysozyme soaked with thiourea 1.5M

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
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 A 201
ChainResidue
AASN65
AASN74
AASN77
AILE78
APRO79
AARG112
ALYS116

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NO3 A 203
ChainResidue
ATRP62
ALYS33
APHE38

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 205
ChainResidue
ASER24
ALEU25
AGLY26
AGLN41
AGLN121
AILE124

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 206
ChainResidue
ATYR23
AARG45
AARG68
AGLY104
AMET105
AASN106

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 300
ChainResidue
ATYR20
AARG21
AALA110
AASN113
AARG114
AHOH333

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE TOU A 221
ChainResidue
AGLN57
AASN59
ATRP63
AALA107
ATRP108
AHOH355

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE TOU A 222
ChainResidue
AARG45
ACYS76
AASN77
AHOH356

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE TOU A 223
ChainResidue
AASN65
ASER81
AASN113

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 Residues2
DetailsACT_SITE:
ChainResidueDetails
AGLU35
AASP52

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AASP101

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 132l
ChainResidueDetails
AGLU35
AASP52

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

221716

PDB entries from 2024-06-26

PDB statisticsPDBj update infoContact PDBjnumon