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4YEO

Triclinic HEWL co-crystallised with cisplatin, studied at a data collection temperature of 150K - new refinement

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 Residues7
Detailsbinding site for residue CPT A 201
ChainResidue
AARG14
AHIS15
AASN37
AARG61
APT202
AHOH429
AHOH497

site_idAC2
Number of Residues2
Detailsbinding site for residue PT A 202
ChainResidue
AHIS15
ACPT201

site_idAC3
Number of Residues2
Detailsbinding site for residue PT A 203
ChainResidue
AHIS15
AHOH430

site_idAC4
Number of Residues2
Detailsbinding site for residue PT A 204
ChainResidue
ALYS116
ANO3210

site_idAC5
Number of Residues4
Detailsbinding site for residue PT A 205
ChainResidue
ALYS1
ASER86
AHOH361
AHOH423

site_idAC6
Number of Residues12
Detailsbinding site for residue EDO A 206
ChainResidue
APRO79
ASER81
AALA82
AARG112
AASN113
AARG114
ACYS115
ALYS116
ATHR118
AHOH301
AHOH425
AHOH498

site_idAC7
Number of Residues7
Detailsbinding site for residue DMS A 207
ChainResidue
AGLN57
AILE58
AASN59
ATRP63
AALA107
ATRP108
AHOH515

site_idAC8
Number of Residues8
Detailsbinding site for residue DMS A 208
ChainResidue
AARG21
AASN65
AASP66
AGLY67
ANO3209
ANO3210
AHOH373
AHOH380

site_idAC9
Number of Residues8
Detailsbinding site for residue NO3 A 209
ChainResidue
AARG21
AASP66
APRO79
ACYS80
ASER81
ADMS208
AHOH349
AHOH367

site_idAD1
Number of Residues9
Detailsbinding site for residue NO3 A 210
ChainResidue
AASN65
AASN74
AASN77
AILE78
APRO79
ALYS116
APT204
ADMS208
AHOH325

site_idAD2
Number of Residues8
Detailsbinding site for residue NO3 A 211
ChainResidue
ASER24
ALEU25
AGLY26
AGLN41
AGLN121
AILE124
AHOH350
AHOH397

site_idAD3
Number of Residues5
Detailsbinding site for residue NO3 A 212
ChainResidue
APHE34
ALYS96
AARG114
AHOH386
AHOH395

site_idAD4
Number of Residues8
Detailsbinding site for residue NO3 A 213
ChainResidue
ATYR23
AARG45
AMET105
AASN106
ATRP111
AHOH310
AHOH327
AHOH364

site_idAD5
Number of Residues7
Detailsbinding site for residue NO3 A 214
ChainResidue
AASN46
ATHR47
AASP48
ALYS97
AHOH313
AHOH338
AHOH468

site_idAD6
Number of Residues8
Detailsbinding site for residue NO3 A 215
ChainResidue
ATHR69
APRO70
AGLY71
ASER72
AGLN121
AARG125
AHOH357
AHOH502

site_idAD7
Number of Residues7
Detailsbinding site for residue ACT A 216
ChainResidue
ATRP62
AARG73
ATRP123
AHOH324
AHOH459
ALYS33
APHE38

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
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
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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