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6GOI

X-ray structure of the adduct formed upon reaction of lysozyme with a Pd(II) complex bearing N,N-pyridylbenzimidazole derivative with an alkylated triphenylphosphonium cation

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
A0008152biological_processmetabolic process
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 Residues7
Detailsbinding site for residue NO3 A 401
ChainResidue
ASER24
ALEU25
AGLY26
AVAL120
AGLN121
AILE124
AHOH515

site_idAC2
Number of Residues5
Detailsbinding site for residue NO3 A 402
ChainResidue
AASN77
AILE78
APRO79
AASN65
AASN74

site_idAC3
Number of Residues4
Detailsbinding site for residue NO3 A 403
ChainResidue
ATRP62
ATRP63
ADMS412
AHOH517

site_idAC4
Number of Residues4
Detailsbinding site for residue NO3 A 404
ChainResidue
AARG5
ALYS33
APHE38
ATRP123

site_idAC5
Number of Residues9
Detailsbinding site for residue NO3 A 405
ChainResidue
ACYS64
AASN65
AASP66
AGLY67
AARG68
ATHR69
ASER72
AHOH502
AHOH505

site_idAC6
Number of Residues9
Detailsbinding site for residue NO3 A 406
ChainResidue
AARG21
AVAL99
ASER100
AGLY102
AASN103
AGLY104
AVAL109
AASN113
AHOH504

site_idAC7
Number of Residues5
Detailsbinding site for residue PD A 407
ChainResidue
AARG14
AHIS15
AASP87
AHOH563
AHOH580

site_idAC8
Number of Residues4
Detailsbinding site for residue PD A 408
ChainResidue
AHIS15
ACL409
ACL410
ADMS411

site_idAC9
Number of Residues4
Detailsbinding site for residue CL A 409
ChainResidue
AHIS15
AASN93
APD408
ACL410

site_idAD1
Number of Residues3
Detailsbinding site for residue CL A 410
ChainResidue
APD408
ACL409
ADMS411

site_idAD2
Number of Residues5
Detailsbinding site for residue DMS A 411
ChainResidue
AARG14
AHIS15
AARG128
APD408
ACL410

site_idAD3
Number of Residues5
Detailsbinding site for residue DMS A 412
ChainResidue
AGLN57
AASN59
ATRP63
AALA107
ANO3403

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

218500

PDB entries from 2024-04-17

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