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4OOT

X-ray structure of the protein-gold adduct formed upon reaction of Aubipic with hen egg white lysozyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0016231molecular_functionbeta-N-acetylglucosaminidase activity
A0016787molecular_functionhydrolase 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 Residues3
DetailsBINDING SITE FOR RESIDUE AU A 201
ChainResidue
ATRP62
AGLN121
AHOH301

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 202
ChainResidue
ANO3207
AHOH403
AGLN57
AILE58
AASN59
ATRP63
AALA107
ATRP108

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 203
ChainResidue
ATRP123
ANO3208

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 204
ChainResidue
ASER24
ALEU25
AGLY26
AVAL120
AGLN121
AILE124

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 A 205
ChainResidue
AALA11
AARG14
AHIS15
ASER86
AASP87
AILE88
AHOH330
AHOH383

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO3 A 206
ChainResidue
AASN65
AASN74
AASN77
AILE78
APRO79

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 A 207
ChainResidue
AASN59
ATRP62
ATRP63
AILE98
AEDO202
AHOH362
AHOH367

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO3 A 208
ChainResidue
AARG5
ALYS33
APHE38
ATRP123
AEDO203

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NO3 A 209
ChainResidue
ACYS64
AASN65
AASP66
AGLY67
AARG68
ATHR69
ASER72
AHOH337
AHOH360

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NO3 A 210
ChainResidue
AARG21
AVAL99
ASER100
AGLY102
AASN103
AGLY104
AVAL109
AASN113
AHOH361

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

237735

PDB entries from 2025-06-18

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