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3MOY

Crystal structure of probable enoyl-CoA hydratase from Mycobacterium smegmatis

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
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SO4 A 260
ChainResidue
AHOH277
AHOH365
AHOH365
AHOH365
AHOH277
AHOH277
AHOH294
AHOH294
AHOH294
AHOH314
AHOH314
AHOH314

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE TRS A 261
ChainResidue
AGLU218
AGLU218
AGLU218
AARG219
AARG219
AARG219
APRO220
APRO220
APRO220
AHOH294
AHOH294
AHOH294
AHOH324
AHOH324
AHOH324

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 262
ChainResidue
AGLY110
AGLU113
AGLU133
APRO140
AGLY141
ALEU142
AEDO263

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 263
ChainResidue
AGLY66
AALA67
AGLY109
AGLY110
APRO132
AEDO262
AHOH488

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 264
ChainResidue
ASER10
AARG11

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 265
ChainResidue
ATHR168
AGLU170
AARG174
AHOH430

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 267
ChainResidue
ALEU75
APHE236
AGLN241
AHOH427
AHOH498

Functional Information from PROSITE/UniProt
site_idPS00166
Number of Residues21
DetailsENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. VAaVAGyalGGGcelaMlCDL
ChainResidueDetails
AVAL100-LEU120

218853

PDB entries from 2024-04-24

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