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4FZW

Crystal Structure of the PaaF-PaaG Hydratase-Isomerase Complex from E.coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004300molecular_functionenoyl-CoA hydratase activity
A0005515molecular_functionprotein binding
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0010124biological_processphenylacetate catabolic process
A0016829molecular_functionlyase activity
A0042802molecular_functionidentical protein binding
A1902494cellular_componentcatalytic complex
B0003824molecular_functioncatalytic activity
B0004300molecular_functionenoyl-CoA hydratase activity
B0005515molecular_functionprotein binding
B0006631biological_processfatty acid metabolic process
B0006635biological_processfatty acid beta-oxidation
B0010124biological_processphenylacetate catabolic process
B0016829molecular_functionlyase activity
B0042802molecular_functionidentical protein binding
B1902494cellular_componentcatalytic complex
C0005515molecular_functionprotein binding
C0006635biological_processfatty acid beta-oxidation
C0010124biological_processphenylacetate catabolic process
C0016829molecular_functionlyase activity
C0016853molecular_functionisomerase activity
C0042802molecular_functionidentical protein binding
C1902494cellular_componentcatalytic complex
D0005515molecular_functionprotein binding
D0006635biological_processfatty acid beta-oxidation
D0010124biological_processphenylacetate catabolic process
D0016829molecular_functionlyase activity
D0016853molecular_functionisomerase activity
D0042802molecular_functionidentical protein binding
D1902494cellular_componentcatalytic complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
AMET68
AARG81
AGLU109
AGLU129

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL B 301
ChainResidue
BARG23
BPHE58

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 302
ChainResidue
BGLU129
BGLY137
BARG81
BTRP85
BGLU109

Functional Information from PROSITE/UniProt
site_idPS00166
Number of Residues21
DetailsENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. IAaVNGyalGAGcelaLlCDV
ChainResidueDetails
AILE96-VAL116

226262

PDB entries from 2024-10-16

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