1CTS

CRYSTALLOGRAPHIC REFINEMENT AND ATOMIC MODELS OF TWO DIFFERENT FORMS OF CITRATE SYNTHASE AT 2.7 AND 1.7 ANGSTROMS RESOLUTION

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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
A0005759cellular_componentmitochondrial matrix
A0004108molecular_functioncitrate (Si)-synthase activity
A0036440molecular_functioncitrate synthase activity
A0005975biological_processcarbohydrate metabolic process
A0006099biological_processtricarboxylic acid cycle
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PDBデータベースに由来する情報

site_id残基数詳細
AC14BINDING SITE FOR RESIDUE CIT A 438
鎖名残基
AHIS238
AASN242
AHIS274
AARG401

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「HETATM」原子の座標から抽出されたリガンド結合部位

site_id残基数詳細
CIT_1cts_A_4387CITRIC ACID binding site
鎖名残基ligand
AHIS238CIT: CITRIC ACID
AASN242CIT: CITRIC ACID
ALEU273-HIS274CIT: CITRIC ACID
AARG329CIT: CITRIC ACID
APHE397CIT: CITRIC ACID
AARG401CIT: CITRIC ACID

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UniProtにおけるモチーフ・データベースPROSITEからの機能情報

site_id残基数詳細
PS0048013Citrate synthase signature. G-[FYAV]-[GA]-H-x-[IV]-x(1,2)-[RKTQ]-x(2)-[DV]-[PS]-R
鎖名残基詳細
AGLY317-ARG329

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SwissProt/UniProtに記載されている蛋白質分子機能情報

site_id残基数詳細
SWS_FT_FI13
鎖名残基詳細
AHIS274
AHIS320
AASP375

extCATRES13Mapped from 1al6 to 1cts using BLAST. All catalytic residues present. Original details record follows: a catalytic site defined by CATRES, Medline 90248434
鎖名残基詳細
AASP375acid/base. removes proton from CH3 group, leading to enolisation of substrate
AHIS274acid/base. donates proton to carbonyl group of substrate, then deprotonates same group
AHIS320acid/base. donates proton to carbonyl group of substrate

CSA13Annotated By Reference To The Literature 1aj8
鎖名残基詳細
AASP375
AHIS274
AHIS320

CSA24Annotated By Reference To The Literature 1aj8
鎖名残基詳細
AASP375
AHIS320
AHIS274
ASER244

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CSAにおける酵素触媒機能の情報

site_id残基数詳細
CSA13Annotated By Reference To The Literature 1aj8
鎖名残基詳細
AASP375
AHIS274
AHIS320

CSA24Annotated By Reference To The Literature 1aj8
鎖名残基詳細
AASP375
AHIS320
AHIS274
ASER244