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3TLF

Crystal structure of an enoyl-CoA hydratase/isomerase from Mycobacterium paratuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004300molecular_functionenoyl-CoA hydratase activity
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0016829molecular_functionlyase activity
B0003824molecular_functioncatalytic activity
B0004300molecular_functionenoyl-CoA hydratase activity
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006635biological_processfatty acid beta-oxidation
B0016829molecular_functionlyase activity
C0003824molecular_functioncatalytic activity
C0004300molecular_functionenoyl-CoA hydratase activity
C0006629biological_processlipid metabolic process
C0006631biological_processfatty acid metabolic process
C0006635biological_processfatty acid beta-oxidation
C0016829molecular_functionlyase activity
D0003824molecular_functioncatalytic activity
D0004300molecular_functionenoyl-CoA hydratase activity
D0006629biological_processlipid metabolic process
D0006631biological_processfatty acid metabolic process
D0006635biological_processfatty acid beta-oxidation
D0016829molecular_functionlyase activity
E0003824molecular_functioncatalytic activity
E0004300molecular_functionenoyl-CoA hydratase activity
E0006629biological_processlipid metabolic process
E0006631biological_processfatty acid metabolic process
E0006635biological_processfatty acid beta-oxidation
E0016829molecular_functionlyase activity
F0003824molecular_functioncatalytic activity
F0004300molecular_functionenoyl-CoA hydratase activity
F0006629biological_processlipid metabolic process
F0006631biological_processfatty acid metabolic process
F0006635biological_processfatty acid beta-oxidation
F0016829molecular_functionlyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO D 271
ChainResidue
DGLU176
DARG182
DHOH285
DHOH298
DHOH306
DHOH318

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO E 271
ChainResidue
DGLU176
EARG201

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO E 272
ChainResidue
EGLU176
EARG182
EHOH283
EHOH299
EHOH327
EHOH407
EARG168

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO F 271
ChainResidue
EHIS175
EGLU176
FARG201
FILE208
FHOH849

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO F 272
ChainResidue
FILE165
FARG168
FGLU176
FARG182
FHOH287
FHOH292
FHOH299
FHOH301

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 271
ChainResidue
AARG168
AGLU176
AHOH288
AHOH308
AHOH592

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 271
ChainResidue
BARG168
BGLU176
BARG182
BHOH286
BHOH308
BHOH316
BHOH390

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO C 271
ChainResidue
AHOH287
CILE165
CHOH288
CHOH297
CHOH410

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 272
ChainResidue
BGLN96
BPRO101
BPHE102
BARG103

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO D 272
ChainResidue
DARG201
DILE208
FHIS175
FGLU176

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 272
ChainResidue
AHIS44
ATHR104

Functional Information from PROSITE/UniProt
site_idPS00166
Number of Residues21
DetailsENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. LTaVNGiccGAGmdwvTtTDI
ChainResidueDetails
ALEU110-ILE130

250359

PDB entries from 2026-03-11

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