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3R0O

Crystal structure of carnitinyl-CoA hydratase from Mycobacterium avium

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004300molecular_functionenoyl-CoA hydratase activity
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
B0003824molecular_functioncatalytic activity
B0004300molecular_functionenoyl-CoA hydratase activity
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
C0003824molecular_functioncatalytic activity
C0004300molecular_functionenoyl-CoA hydratase activity
C0016829molecular_functionlyase activity
C0016836molecular_functionhydro-lyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 270
ChainResidue
ATYR97
AHIS100
ATHR106
AALA124
AHOH280

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 270
ChainResidue
BHOH300
BTYR97
BHIS100
BTHR106
BALA124

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO C 270
ChainResidue
CTYR97
CHIS100
CILE102
CTHR106
CALA124
CHOH279
CHOH311

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 271
ChainResidue
BASN186
BGLU187
BARG204
BHOH552
CGLU166

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 271
ChainResidue
AARG181
ATRP182
BARG181
CARG181

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 272
ChainResidue
BPHE94
BGLY117
BGLU120
BGLU140
BILE146
BGLY148
BALA149
BPHE242

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE K C 271
ChainResidue
CGLU120
CGLU140

Functional Information from PROSITE/UniProt
site_idPS00166
Number of Residues21
DetailsENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. IAaVNGtalGGGselaLaSDL
ChainResidueDetails
AILE107-LEU127

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PDB entries from 2024-07-10

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