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5OB6

X-ray structure of the adduct formed upon reaction of lysozyme with the compound fac-[RuII(CO)3Cl2(N3-IM), IM=imidazole

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 GOL A 201
ChainResidue
ALYS13
ALYS13
ALEU129
ALEU129
ARU2209
ARU2209

site_idAC2
Number of Residues2
Detailsbinding site for residue CL A 202
ChainResidue
ATYR23
AASN113

site_idAC3
Number of Residues6
Detailsbinding site for residue NA A 203
ChainResidue
ACYS64
ASER72
AARG73
AHOH379
AHOH380
ASER60

site_idAC4
Number of Residues7
Detailsbinding site for residue CL A 204
ChainResidue
AASN65
AGLY67
AARG68
ATHR69
AHOH380
AHOH400
AHOH417

site_idAC5
Number of Residues6
Detailsbinding site for residue 9Q8 A 205
ChainResidue
AALA11
AHIS15
AASP87
AILE88
ATHR89
AHOH395

site_idAC6
Number of Residues6
Detailsbinding site for residue RU2 A 206
ChainResidue
ALYS13
AASP18
ALEU25
AARG61
APRO70
AILE124

site_idAC7
Number of Residues4
Detailsbinding site for residue RU2 A 207
ChainResidue
AASN46
AASP52
AHOH316
AHOH349

site_idAC8
Number of Residues2
Detailsbinding site for residue RU1 A 208
ChainResidue
AASP119
AARG125

site_idAC9
Number of Residues4
Detailsbinding site for residue RU2 A 209
ChainResidue
ALEU129
ALEU129
AGOL201
AGOL201

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

223166

PDB entries from 2024-07-31

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