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5DL9

Structure of Tetragonal Lysozyme in complex with Iodine solved by UWO Students

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 Residues3
Detailsbinding site for residue IOD A 201
ChainResidue
AASN44
AARG68
AEDO213

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

site_idAC3
Number of Residues1
Detailsbinding site for residue IOD A 203
ChainResidue
ALYS33

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO A 205
ChainResidue
ATHR118
AHOH338
AASN27
AARG114
AGLY117

site_idAC5
Number of Residues9
Detailsbinding site for residue EDO A 206
ChainResidue
AARG21
AGLU35
AVAL109
AEDO207
AEDO210
AEDO211
AEDO212
AACT214
AHOH304

site_idAC6
Number of Residues10
Detailsbinding site for residue EDO A 207
ChainResidue
AARG21
AGLY22
AGLU35
AASN44
AGLN57
AEDO206
AEDO211
AEDO213
AHOH304
AHOH312

site_idAC7
Number of Residues7
Detailsbinding site for residue EDO A 208
ChainResidue
AGLN57
AILE58
AASN59
AALA107
ATRP108
AHOH319
AHOH320

site_idAC8
Number of Residues7
Detailsbinding site for residue EDO A 209
ChainResidue
AASN46
AASP48
ASER50
AEDO210
AHOH323
AHOH327
AHOH361

site_idAC9
Number of Residues9
Detailsbinding site for residue EDO A 210
ChainResidue
AARG21
AASN46
AVAL109
AEDO206
AEDO209
AEDO211
AACT214
AHOH302
AHOH346

site_idAD1
Number of Residues9
Detailsbinding site for residue EDO A 211
ChainResidue
AARG21
AASN44
AASN46
AASP52
AEDO206
AEDO207
AEDO210
AHOH302
AHOH312

site_idAD2
Number of Residues9
Detailsbinding site for residue EDO A 212
ChainResidue
AARG21
AVAL99
ASER100
AASP101
AGLY102
AASN103
AGLY104
AVAL109
AEDO206

site_idAD3
Number of Residues9
Detailsbinding site for residue EDO A 213
ChainResidue
AASN19
AGLY22
APHE34
AGLU35
ASER36
AASN37
AIOD201
AEDO207
AHOH303

site_idAD4
Number of Residues10
Detailsbinding site for residue ACT A 214
ChainResidue
AGLU35
AASP52
AGLN57
AALA107
ATRP108
AVAL109
AALA110
AEDO206
AEDO210
AHOH319

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

218853

PDB entries from 2024-04-24

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