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8BIT

Crystal structure of acyl-CoA synthetase from Metallosphaera sedula in complex with Coenzyme A and acetyl-AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003987molecular_functionacetate-CoA ligase activity
A0004321molecular_functionfatty-acyl-CoA synthase activity
A0005524molecular_functionATP binding
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0006637biological_processacyl-CoA metabolic process
A0015645molecular_functionfatty acid ligase activity
A0016020cellular_componentmembrane
A0016405molecular_functionCoA-ligase activity
A0016874molecular_functionligase activity
A0016878molecular_functionacid-thiol ligase activity
A0031956molecular_functionmedium-chain fatty acid-CoA ligase activity
A0050218molecular_functionpropionate-CoA ligase activity
B0003987molecular_functionacetate-CoA ligase activity
B0004321molecular_functionfatty-acyl-CoA synthase activity
B0005524molecular_functionATP binding
B0006631biological_processfatty acid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0006637biological_processacyl-CoA metabolic process
B0015645molecular_functionfatty acid ligase activity
B0016020cellular_componentmembrane
B0016405molecular_functionCoA-ligase activity
B0016874molecular_functionligase activity
B0016878molecular_functionacid-thiol ligase activity
B0031956molecular_functionmedium-chain fatty acid-CoA ligase activity
B0050218molecular_functionpropionate-CoA ligase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
BVAL111-PRO131
AVAL111-PRO131

site_idSWS_FT_FI2
Number of Residues22
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q08AH3
ChainResidueDetails
BTHR210
BVAL527
BLYS544
ATHR210
AASP349
ATHR354
AASP435
AARG450
ASER458
AARG461
AARG490
BASP349
ALYS519
AVAL527
ALYS544
BTHR354
BASP435
BARG450
BSER458
BARG461
BARG490
BLYS519

227561

PDB entries from 2024-11-20

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