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6SET

X-ray structure of the gold/lysozyme adduct formed upon 3 days exposure of protein crystals to compound 1

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 Residues8
Detailsbinding site for residue NO3 A 201
ChainResidue
AALA11
AARG14
AHIS15
ASER86
AASP87
AILE88
ANO3203
AHOH319

site_idAC2
Number of Residues10
Detailsbinding site for residue NO3 A 202
ChainResidue
AASN65
AASP66
AGLY67
AARG68
ATHR69
ASER72
AHOH301
AHOH317
AHOH358
ACYS64

site_idAC3
Number of Residues5
Detailsbinding site for residue NO3 A 203
ChainResidue
AALA10
AALA10
AARG14
AARG14
ANO3201

site_idAC4
Number of Residues10
Detailsbinding site for residue NO3 A 204
ChainResidue
AASN19
AGLU35
ASER36
AALA42
AASN44
AARG68
ANO3207
AAU210
AAU211
AHOH345

site_idAC5
Number of Residues9
Detailsbinding site for residue NO3 A 205
ChainResidue
AASN27
APHE34
ATRP111
AARG114
ALYS116
AGLY117
AAU212
AHOH305
AHOH309

site_idAC6
Number of Residues3
Detailsbinding site for residue EDO A 206
ChainResidue
AARG5
AALA122
ATRP123

site_idAC7
Number of Residues9
Detailsbinding site for residue NO3 A 207
ChainResidue
AASN19
AARG21
AGLY22
AASN44
ANO3204
AAU211
ANA213
AHOH313
AHOH369

site_idAC8
Number of Residues6
Detailsbinding site for residue DMS A 208
ChainResidue
AGLN57
AILE58
AASN59
ATRP63
AALA107
ATRP108

site_idAC9
Number of Residues3
Detailsbinding site for residue CL A 209
ChainResidue
ACYS76
AASN77
AILE78

site_idAD1
Number of Residues6
Detailsbinding site for residue AU A 210
ChainResidue
AASN19
AGLY22
APHE34
AASN37
ANO3204
AHOH401

site_idAD2
Number of Residues6
Detailsbinding site for residue AU A 211
ChainResidue
AASN19
AASN44
AARG45
ANO3204
ANO3207
AHOH306

site_idAD3
Number of Residues4
Detailsbinding site for residue AU A 212
ChainResidue
ATHR118
ANO3205
AHOH305
AHOH416

site_idAD4
Number of Residues6
Detailsbinding site for residue NA A 213
ChainResidue
AGLU35
ANO3207
AHOH312
AHOH313
AHOH369
AHOH383

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

225946

PDB entries from 2024-10-09

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