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5I4Y

Exploring onset of lysozyme denaturation by urea: soak period 10 hours.

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
A0005794cellular_componentGolgi apparatus
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 URE A 201
ChainResidue
AALA10
AALA10
AARG14
AARG14
ALEU129
ALEU129

site_idAC2
Number of Residues7
Detailsbinding site for residue URE A 202
ChainResidue
AARG45
AARG68
AHOH374
AHOH374
ATHR43
ATHR43
AARG45

site_idAC3
Number of Residues3
Detailsbinding site for residue URE A 203
ChainResidue
ACYS6
AARG128
AHOH355

site_idAC4
Number of Residues5
Detailsbinding site for residue URE A 204
ChainResidue
AARG61
AILE124
ACYS127
ALEU129
AHOH367

site_idAC5
Number of Residues6
Detailsbinding site for residue URE A 205
ChainResidue
AASN65
AGLY67
AARG68
ATHR69
ASER72
AHOH330

site_idAC6
Number of Residues7
Detailsbinding site for residue URE A 206
ChainResidue
AGLN57
AILE58
AASN59
ATRP63
AALA107
ATRP108
AURE209

site_idAC7
Number of Residues6
Detailsbinding site for residue URE A 207
ChainResidue
APHE34
ATRP111
AARG114
AGLY117
AURE211
AURE216

site_idAC8
Number of Residues6
Detailsbinding site for residue URE A 208
ChainResidue
ALYS13
APRO70
APRO70
AHOH360
AHOH365
AHOH367

site_idAC9
Number of Residues9
Detailsbinding site for residue URE A 209
ChainResidue
AGLU35
AASP52
AGLN57
AALA107
ATRP108
AVAL109
AURE206
AHOH334
AHOH352

site_idAD1
Number of Residues4
Detailsbinding site for residue URE A 210
ChainResidue
AASN37
AASN39
AGLY67
AHOH370

site_idAD2
Number of Residues7
Detailsbinding site for residue URE A 211
ChainResidue
AARG114
ATHR118
AASP119
ATRP123
AURE207
AHOH313
AHOH363

site_idAD3
Number of Residues4
Detailsbinding site for residue URE A 212
ChainResidue
AARG21
AASN46
ATHR47
AURE214

site_idAD4
Number of Residues4
Detailsbinding site for residue URE A 213
ChainResidue
ALYS33
AURE221
AHOH301
AHOH335

site_idAD5
Number of Residues7
Detailsbinding site for residue URE A 214
ChainResidue
AARG21
AARG45
AASN46
AASP52
AURE212
AHOH311
AHOH346

site_idAD6
Number of Residues4
Detailsbinding site for residue URE A 215
ChainResidue
ALYS33
APHE38
ACL222
AHOH371

site_idAD7
Number of Residues7
Detailsbinding site for residue URE A 216
ChainResidue
AASN27
AARG114
ATHR118
AVAL120
AURE207
AURE221
AHOH301

site_idAD8
Number of Residues5
Detailsbinding site for residue URE A 217
ChainResidue
AARG45
AGLY49
AURE219
AHOH306
AHOH377

site_idAD9
Number of Residues4
Detailsbinding site for residue URE A 218
ChainResidue
AHOH312
AHOH348
AARG5
ACYS6

site_idAE1
Number of Residues9
Detailsbinding site for residue URE A 219
ChainResidue
AGLY16
AASP18
AASN19
ATYR20
AARG45
AURE217
AHOH305
AHOH318
AHOH368

site_idAE2
Number of Residues5
Detailsbinding site for residue URE A 220
ChainResidue
AASN19
AGLY22
APHE34
AGLU35
AURE221

site_idAE3
Number of Residues10
Detailsbinding site for residue URE A 221
ChainResidue
AGLY22
ATYR23
ASER24
AASN27
AARG114
AURE213
AURE216
AURE220
AHOH301
AHOH303

site_idAE4
Number of Residues2
Detailsbinding site for residue CL A 222
ChainResidue
AARG5
AURE215

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 Residues128
DetailsDomain: {"description":"C-type lysozyme","evidences":[{"source":"PROSITE-ProRule","id":"PRU00680","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {}
ChainResidueDetails

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

247536

PDB entries from 2026-01-14

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