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5XUW

Crystal structure of lysozyme from Equus asinus

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0046872molecular_functionmetal ion binding
B0003796molecular_functionlysozyme activity
B0003824molecular_functioncatalytic activity
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0031640biological_processkilling of cells of another organism
B0042742biological_processdefense response to bacterium
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue CA A 201
ChainResidue
ALYS82
AASP85
AASN87
AASP90
AASP91
AHOH310
AHOH334

site_idAC2
Number of Residues7
Detailsbinding site for residue CA B 201
ChainResidue
BASN87
BASP90
BASP91
BHOH311
BHOH332
BLYS82
BASP85

Functional Information from PROSITE/UniProt
site_idPS00128
Number of Residues19
DetailsGLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CnimCskLlddNIdddisC
ChainResidueDetails
ACYS76-CYS94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues256
DetailsDomain: {"description":"C-type lysozyme","evidences":[{"source":"PROSITE-ProRule","id":"PRU00680","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00680","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P81708","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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