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3R9S

Structure of a carnitinyl-CoA dehydratase from Mycobacterium avium 104

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004300molecular_functionenoyl-CoA hydratase activity
A0006635biological_processfatty acid beta-oxidation
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
B0003824molecular_functioncatalytic activity
B0004300molecular_functionenoyl-CoA hydratase activity
B0006635biological_processfatty acid beta-oxidation
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
C0003824molecular_functioncatalytic activity
C0004300molecular_functionenoyl-CoA hydratase activity
C0006635biological_processfatty acid beta-oxidation
C0016829molecular_functionlyase activity
C0016836molecular_functionhydro-lyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BEZ A 264
ChainResidue
AILE72
AGLU114
AGLU134
AILE140
AALA141
AALA142
AALA143
AHOH287

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 265
ChainResidue
ATYR91
AHIS94
AILE96
ATHR100
AALA118
ALEU41

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 264
ChainResidue
BHIS94
BPHE95
BILE96
BTHR100
BALA118
BLYS211

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BEZ C 264
ChainResidue
CILE72
CGLU114
CGLU134
CALA141
CALA142
CALA143
CHOH270

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO C 265
ChainResidue
CTYR91
CHIS94
CILE96
CTHR100
CALA118
CSER119
CHOH297

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO C 266
ChainResidue
CARG148
CGLU151
CGLN152
CTYR215
CASP225
CHOH291
CHOH305

Functional Information from PROSITE/UniProt
site_idPS00166
Number of Residues21
DetailsENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. IAaVNGtalGGGtelaLaSDL
ChainResidueDetails
AILE101-LEU121

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PDB entries from 2024-09-04

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