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2EIS

X-ray structure of acyl-CoA hydrolase-like protein, TT1379, from Thermus thermophilus HB8

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0006631biological_processfatty acid metabolic process
A0006637biological_processacyl-CoA metabolic process
A0016787molecular_functionhydrolase activity
A0016790molecular_functionthiolester hydrolase activity
A0036042molecular_functionlong-chain fatty acyl-CoA binding
A0047617molecular_functionfatty acyl-CoA hydrolase activity
B0005829cellular_componentcytosol
B0006631biological_processfatty acid metabolic process
B0006637biological_processacyl-CoA metabolic process
B0016787molecular_functionhydrolase activity
B0016790molecular_functionthiolester hydrolase activity
B0036042molecular_functionlong-chain fatty acyl-CoA binding
B0047617molecular_functionfatty acyl-CoA hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE COA A 201
ChainResidue
ATHR48
AHOH228
AHOH236
AHOH272
AHOH296
AHOH306
AHOH319
BLEU21
BGLY23
BASP55
BPHE56
AHIS50
BLYS57
BARG58
BPRO59
BHOH300
BHOH319
AARG58
AGLY76
AARG77
ATHR78
ASER79
AARG102
AHOH205

site_idAC2
Number of Residues26
DetailsBINDING SITE FOR RESIDUE COA B 202
ChainResidue
ALEU21
AGLY23
AASP55
APHE56
ALYS57
AARG58
APRO59
AHOH204
AHOH325
BTHR48
BHIS50
BARG58
BGLY76
BARG77
BTHR78
BSER79
BARG102
BPRO116
BHOH203
BHOH205
BHOH235
BHOH264
BHOH270
BHOH279
BHOH283
BHOH310

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PDB entries from 2024-04-24

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