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2MEG

CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS.

GO(遺伝子オントロジー)由来の情報
鎖名GO(遺伝子オントロジー)id名前空間内容
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006954biological_processinflammatory response
A0008152biological_processmetabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0019730biological_processantimicrobial humoral response
A0031640biological_processkilling of cells of another organism
A0035578cellular_componentazurophil granule lumen
A0035580cellular_componentspecific granule lumen
A0042742biological_processdefense response to bacterium
A0042802molecular_functionidentical protein binding
A0050829biological_processdefense response to Gram-negative bacterium
A0050830biological_processdefense response to Gram-positive bacterium
A0070062cellular_componentextracellular exosome
A1904724cellular_componenttertiary granule lumen
PDBデータベースに由来する情報
site_idAC1
残基数6
詳細BINDING SITE FOR RESIDUE NA A 601
鎖名残基
ASER61
ACYS65
AALA73
AVAL74
AHOH135
AHOH157

UniProtにおけるモチーフ・データベースPROSITEからの機能情報
site_idPS00128
残基数19
詳細GLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. ChlsCsaLlqdNIadavaC
鎖名残基詳細
ACYS77-CYS95

SwissProt/UniProtに記載されている蛋白質分子機能情報
site_idSWS_FT_FI1
残基数2
詳細ACT_SITE:
鎖名残基詳細
AGLU35
AASP53

218500

件を2024-04-17に公開中

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