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4Z41

X-ray structure of the adduct formed in the reaction between lysozyme and a platinum(II) Compound with a S,O Bidentate Ligand (9a=Chloro-(1-(3'-hydroxy)-3-(methylthio)-3-thioxo-prop-1-en-1-olate-O,S)-(dimethylsulfoxide-S)-platinum(II))

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
AVAL92
AASN93
ALYS96
AARG128
AHOH305

site_idAC2
Number of Residues2
Detailsbinding site for residue DMS A 202
ChainResidue
ATRP62
ALEU75

site_idAC3
Number of Residues9
Detailsbinding site for residue NO3 A 203
ChainResidue
ACYS64
AASN65
AASP66
AGLY67
AARG68
ATHR69
ASER72
AHOH302
AHOH304

site_idAC4
Number of Residues7
Detailsbinding site for residue NO3 A 204
ChainResidue
AGLY22
ASER24
AASN27
APHE34
AARG114
AVAL120
AEDO211

site_idAC5
Number of Residues7
Detailsbinding site for residue NO3 A 205
ChainResidue
APHE3
AARG14
AHIS15
ASER86
AASP87
AILE88
AHOH316

site_idAC6
Number of Residues6
Detailsbinding site for residue NO3 A 206
ChainResidue
AARG5
ALYS33
APHE38
AEDO208
AHOH356
AHOH371

site_idAC7
Number of Residues5
Detailsbinding site for residue NO3 A 207
ChainResidue
AASN65
AASN74
AASN77
AILE78
APRO79

site_idAC8
Number of Residues3
Detailsbinding site for residue EDO A 208
ChainResidue
AARG5
AALA122
ANO3206

site_idAC9
Number of Residues6
Detailsbinding site for residue EDO A 209
ChainResidue
AGLN57
AILE58
AASN59
AALA107
ATRP108
AHOH321

site_idAD1
Number of Residues5
Detailsbinding site for residue EDO A 210
ChainResidue
ATHR43
ATHR43
ATHR51
AARG68
AARG68

site_idAD2
Number of Residues10
Detailsbinding site for residue EDO A 211
ChainResidue
AASN27
ATRP111
AARG114
ACYS115
AGLY117
ATHR118
AVAL120
ANO3204
AHOH314
AHOH319

site_idAD3
Number of Residues5
Detailsbinding site for residue EDO A 212
ChainResidue
AARG61
ATRP62
AGLY71
AARG73
AHOH309

site_idAD4
Number of Residues5
Detailsbinding site for residue NO3 A 213
ChainResidue
AALA10
AALA10
AARG14
AARG14
ALEU129

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

222926

PDB entries from 2024-07-24

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