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2EQL

CRYSTALLOGRAPHIC STUDIES OF A CALCIUM BINDING LYSOZYME FROM EQUINE MILK AT 2.5 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00128
Number of Residues19
DetailsGLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CnimCskLldeNIdddisC
ChainResidueDetails
ACYS76-CYS94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00680
ChainResidueDetails
AGLU35
AASP53

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:3666156
ChainResidueDetails
ALYS82
AASP85
AASN87
AASP90
AASP91

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 8535779
ChainResidueDetails
AGLU35
AASP53

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PDB entries from 2024-05-01

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