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

2X0A

MPD-Lysozyme structure at 55.5 keV using a TRIXXEL CsI-aSi based digital imager and the new ESRF U22 undulator source at ID15

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 Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1130
ChainResidue
ATYR23
AASN113

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1131
ChainResidue
ASER24
AGLY26
AGLN121

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 1132
ChainResidue
AARG68
AGLN41
AALA42
ATHR43
ATYR53

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 1133
ChainResidue
AGLY49
ASER50
ATHR51
AASP66
AARG68
ATHR69

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MRD A 1134
ChainResidue
AASN19
AGLY22
ALYS33
APHE34
AASN37
AHOH2122
AHOH2123

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_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

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon