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1SBK

X-RAY STRUCTURE OF YDII_ECOLI NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET ER29.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0009234biological_processmenaquinone biosynthetic process
A0016289molecular_functionacyl-CoA hydrolase activity
A0016787molecular_functionhydrolase activity
A0016790molecular_functionthiolester hydrolase activity
A0042372biological_processphylloquinone biosynthetic process
A0061522molecular_function1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity
B0005777cellular_componentperoxisome
B0005829cellular_componentcytosol
B0009234biological_processmenaquinone biosynthetic process
B0016289molecular_functionacyl-CoA hydrolase activity
B0016787molecular_functionhydrolase activity
B0016790molecular_functionthiolester hydrolase activity
B0042372biological_processphylloquinone biosynthetic process
B0061522molecular_function1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity
C0005777cellular_componentperoxisome
C0005829cellular_componentcytosol
C0009234biological_processmenaquinone biosynthetic process
C0016289molecular_functionacyl-CoA hydrolase activity
C0016787molecular_functionhydrolase activity
C0016790molecular_functionthiolester hydrolase activity
C0042372biological_processphylloquinone biosynthetic process
C0061522molecular_function1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity
D0005777cellular_componentperoxisome
D0005829cellular_componentcytosol
D0009234biological_processmenaquinone biosynthetic process
D0016289molecular_functionacyl-CoA hydrolase activity
D0016787molecular_functionhydrolase activity
D0016790molecular_functionthiolester hydrolase activity
D0042372biological_processphylloquinone biosynthetic process
D0061522molecular_function1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 801
ChainResidue
DHIS106
DGLY108
DSER109
DARG110
DHIS111

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 802
ChainResidue
BHIS111
BHOH574
BHIS106
BGLY108
BSER109
BARG110

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 803
ChainResidue
CHIS106
CGLY108
CSER109
CARG110
CHIS111

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 804
ChainResidue
AHIS106
AGLY108
ASER109
AARG110
AHIS111

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile or proton acceptor => ECO:0000255|HAMAP-Rule:MF_01936, ECO:0000303|PubMed:25010423
ChainResidueDetails
AGLU63
BGLU63
CGLU63
DGLU63

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01936, ECO:0000269|PubMed:25010423
ChainResidueDetails
AGLY82
BHIS89
BHIS106
CGLY82
CHIS89
CHIS106
DGLY82
DHIS89
DHIS106
AHIS89
AHIS106
BGLY82

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PDB entries from 2024-04-17

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