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

4Z3M

X-ray structure of the adduct formed in the reaction between lysozyme and a platinum(II) Complex with S,O Bidentate Ligands (9b)

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 Residues9
Detailsbinding site for residue 4KV A 201
ChainResidue
ACYS6
AARG14
AHIS15
ATHR89
AASN93
ALYS96
AARG128
AHOH308
AHOH322

site_idAC2
Number of Residues1
Detailsbinding site for residue DMS A 202
ChainResidue
AASP101

site_idAC3
Number of Residues4
Detailsbinding site for residue NO3 A 203
ChainResidue
AARG14
AHIS15
AASP87
AILE88

site_idAC4
Number of Residues9
Detailsbinding site for residue NO3 A 204
ChainResidue
ACYS64
AASN65
AASP66
AGLY67
AARG68
ATHR69
ASER72
AHOH302
AHOH303

site_idAC5
Number of Residues8
Detailsbinding site for residue NO3 A 205
ChainResidue
AGLY22
ASER24
AASN27
APHE34
AARG114
AVAL120
AEDO208
AHOH304

site_idAC6
Number of Residues6
Detailsbinding site for residue EDO A 206
ChainResidue
ATHR43
ATHR43
AARG45
AARG45
AARG68
AARG68

site_idAC7
Number of Residues1
Detailsbinding site for residue EDO A 207
ChainResidue
AHOH348

site_idAC8
Number of Residues8
Detailsbinding site for residue EDO A 208
ChainResidue
AASN27
AARG114
ACYS115
AGLY117
ATHR118
AVAL120
ANO3205
AHOH352

site_idAC9
Number of Residues5
Detailsbinding site for residue EDO A 209
ChainResidue
AGLN57
AILE58
AASN59
ATRP63
ATRP108

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

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon