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2F9Y

The Crystal Structure of The Carboxyltransferase Subunit of ACC from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0003989molecular_functionacetyl-CoA carboxylase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006633biological_processfatty acid biosynthetic process
A0009317cellular_componentacetyl-CoA carboxylase complex
A0009329cellular_componentacetate CoA-transferase complex
A0016740molecular_functiontransferase activity
A0016743molecular_functioncarboxyl- or carbamoyltransferase activity
A0016874molecular_functionligase activity
A0042759biological_processlong-chain fatty acid biosynthetic process
A0042802molecular_functionidentical protein binding
A2001295biological_processmalonyl-CoA biosynthetic process
B0003677molecular_functionDNA binding
B0003723molecular_functionRNA binding
B0003729molecular_functionmRNA binding
B0003989molecular_functionacetyl-CoA carboxylase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006417biological_processregulation of translation
B0006633biological_processfatty acid biosynthetic process
B0008270molecular_functionzinc ion binding
B0009317cellular_componentacetyl-CoA carboxylase complex
B0009329cellular_componentacetate CoA-transferase complex
B0016740molecular_functiontransferase activity
B0016743molecular_functioncarboxyl- or carbamoyltransferase activity
B0017148biological_processnegative regulation of translation
B0042759biological_processlong-chain fatty acid biosynthetic process
B0046872molecular_functionmetal ion binding
B2001295biological_processmalonyl-CoA biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 305
ChainResidue
BCYS27
BCYS30
BCYS46
BCYS49

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsZN_FING: C4-type => ECO:0000305
ChainResidueDetails
BCYS27-CYS49

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
BCYS27
BCYS30
BCYS46
BCYS49

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1xny
ChainResidueDetails
AGLY204
ASER205

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1xny
ChainResidueDetails
AGLY207
AGLY206
BGLY204
BGLY205

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PDB entries from 2024-07-24

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