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6GOB

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

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 Residues6
Detailsbinding site for residue PD A 201
ChainResidue
AASP87
ATHR89
AF6Q208
ACL212
AHOH373
AHOH393

site_idAC2
Number of Residues5
Detailsbinding site for residue PD A 202
ChainResidue
AHOH308
AHOH365
AASN77
AF6Q208
ACL213

site_idAC3
Number of Residues10
Detailsbinding site for residue NO3 A 203
ChainResidue
ACYS64
AASN65
AASP66
AGLY67
AARG68
ATHR69
ASER72
AHOH305
AHOH342
AHOH435

site_idAC4
Number of Residues6
Detailsbinding site for residue NO3 A 204
ChainResidue
AALA10
AALA10
ALYS13
AARG14
AARG14
ALEU129

site_idAC5
Number of Residues10
Detailsbinding site for residue F6Q A 205
ChainResidue
AARG5
ASER100
AASP101
AALA122
AARG125
AGLY126
AF6Q207
AHOH322
AHOH367
AHOH375

site_idAC6
Number of Residues13
Detailsbinding site for residue F6Q A 206
ChainResidue
ATRP62
AASP101
AGLY102
AASN103
AGLY117
ATHR118
AASP119
AGLN121
AF6Q207
AHOH302
AHOH309
AHOH326
AHOH348

site_idAC7
Number of Residues11
Detailsbinding site for residue F6Q A 207
ChainResidue
ALYS33
AASN37
ATRP62
ATRP63
AARG73
ALEU75
AASP101
AGLY102
AF6Q205
AF6Q206
AHOH381

site_idAC8
Number of Residues12
Detailsbinding site for residue F6Q A 208
ChainResidue
ALYS1
AASP87
APD201
APD202
ACL212
AHOH315
AHOH330
AHOH359
AHOH365
AHOH373
AHOH383
AHOH412

site_idAC9
Number of Residues10
Detailsbinding site for residue F6Q A 209
ChainResidue
AARG14
AHIS15
ATHR47
AVAL92
AASN93
ALYS96
AARG128
AHOH301
AHOH355
AHOH421

site_idAD1
Number of Residues7
Detailsbinding site for residue SO4 A 210
ChainResidue
ALEU56
AGLN57
AILE58
AASN59
ATRP63
AALA107
ATRP108

site_idAD2
Number of Residues3
Detailsbinding site for residue SO4 A 211
ChainResidue
ALYS116
ALYS116
AGLY117

site_idAD3
Number of Residues4
Detailsbinding site for residue CL A 212
ChainResidue
AASP87
APD201
AF6Q208
AHOH373

site_idAD4
Number of Residues4
Detailsbinding site for residue CL A 213
ChainResidue
AHOH308
AHOH441
AASN77
APD202

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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