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5NJ1

The X-ray structure of the adduct formed in the reaction between hen egg white lysozyme and arsenoplatin-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 Residues6
Detailsbinding site for residue EDO A 201
ChainResidue
AGLN57
AILE58
AASN59
AALA107
ATRP108
ANO3204

site_idAC2
Number of Residues2
Detailsbinding site for residue EDO A 202
ChainResidue
AARG5
AALA122

site_idAC3
Number of Residues6
Detailsbinding site for residue NO3 A 203
ChainResidue
ALEU25
AGLY26
AVAL120
AGLN121
AILE124
ASER24

site_idAC4
Number of Residues4
Detailsbinding site for residue NO3 A 204
ChainResidue
ATRP62
ATRP63
AEDO201
AHOH343

site_idAC5
Number of Residues10
Detailsbinding site for residue NO3 A 205
ChainResidue
ACYS64
AASN65
AASP66
AGLY67
AARG68
ATHR69
ASER72
ANA209
AHOH305
AHOH313

site_idAC6
Number of Residues9
Detailsbinding site for residue NO3 A 206
ChainResidue
AARG21
AVAL99
ASER100
AGLY102
AASN103
AGLY104
AVAL109
AASN113
AHOH331

site_idAC7
Number of Residues6
Detailsbinding site for residue NO3 A 207
ChainResidue
AASN65
AASN74
AASN77
AILE78
APRO79
AHOH301

site_idAC8
Number of Residues8
Detailsbinding site for residue A6R A 208
ChainResidue
AALY1
AGLU7
AARG14
AHIS15
AASP87
ATHR89
AHOH315
AHOH337

site_idAC9
Number of Residues6
Detailsbinding site for residue NA A 209
ChainResidue
ASER60
ACYS64
ASER72
AARG73
ANO3205
AHOH313

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

224572

PDB entries from 2024-09-04

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