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109L

STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME

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
A0008152biological_processmetabolic process
A0009253biological_processpeptidoglycan catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
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 CL A 173
鎖名残基
ATHR142
AASN144
AARG145
AHOH209
AHOH291
AHOH352

site_idAC2
残基数3
詳細BINDING SITE FOR RESIDUE CL A 178
鎖名残基
ALYS135
AHOH215
AHOH220

site_idAC3
残基数2
詳細BINDING SITE FOR RESIDUE BME A 901
鎖名残基
AASP72
ABME902

site_idAC4
残基数4
詳細BINDING SITE FOR RESIDUE BME A 902
鎖名残基
AALA93
AILE100
AHOH195
ABME901

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1
詳細ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
鎖名残基詳細
AGLU11

site_idSWS_FT_FI2
残基数1
詳細ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
鎖名残基詳細
AASP20

site_idSWS_FT_FI3
残基数2
詳細BINDING: BINDING => ECO:0000269|PubMed:8266098
鎖名残基詳細
ALEU32
APHE104

site_idSWS_FT_FI4
残基数2
詳細BINDING: BINDING => ECO:0000303|PubMed:7831309
鎖名残基詳細
ASER117
AASN132

CSAにおける酵素触媒機能の情報
site_idMCSA1
残基数2
詳細M-CSA 921
鎖名残基詳細
AGLU11proton shuttle (general acid/base)
AASP20covalent catalysis

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件を2024-04-17に公開中

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