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6MX9

Lysozyme bound to 3-Aminophenol

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 Residues10
Detailsbinding site for residue EDO A 201
ChainResidue
AGLN57
AHOH407
AILE58
AASN59
ATRP63
AALA107
ATRP108
AHOH310
AHOH315
AHOH322

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 202
ChainResidue
ASER60
ACYS64
ASER72
AARG73
AHOH388
AHOH397

site_idAC3
Number of Residues2
Detailsbinding site for residue NA A 203
ChainResidue
ABEN209
AHOH366

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 204
ChainResidue
AILE88
AHOH495

site_idAC5
Number of Residues2
Detailsbinding site for residue CL A 205
ChainResidue
ATYR23
AASN113

site_idAC6
Number of Residues4
Detailsbinding site for residue CL A 206
ChainResidue
ASER24
AGLY26
AGLN121
AHOH500

site_idAC7
Number of Residues1
Detailsbinding site for residue CL A 207
ChainResidue
ALYS33

site_idAC8
Number of Residues7
Detailsbinding site for residue CL A 208
ChainResidue
AASN65
AGLY67
AARG68
ATHR69
ASER72
AK5V211
AHOH388

site_idAC9
Number of Residues8
Detailsbinding site for residue BEN A 209
ChainResidue
AASN19
AGLY22
ALYS33
APHE34
AGLU35
AASN37
ANA203
AHOH424

site_idAD1
Number of Residues8
Detailsbinding site for residue K5V A 210
ChainResidue
APHE34
AARG114
AGLY117
ATHR118
AASP119
ATRP123
AHOH332
AHOH354

site_idAD2
Number of Residues8
Detailsbinding site for residue K5V A 211
ChainResidue
AGLY67
AARG68
AGLY71
ASER72
ACL208
AHOH301
AHOH317
AHOH351

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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