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4K4C

X-ray crystal structure of E. coli YbdB complexed with phenacyl-CoA

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009239biological_processenterobactin biosynthetic process
A0016289molecular_functionacyl-CoA hydrolase activity
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0016790molecular_functionthiolester hydrolase activity
A0042802molecular_functionidentical protein binding
A0061522molecular_function1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0009239biological_processenterobactin biosynthetic process
B0016289molecular_functionacyl-CoA hydrolase activity
B0016787molecular_functionhydrolase activity
B0016788molecular_functionhydrolase activity, acting on ester bonds
B0016790molecular_functionthiolester hydrolase activity
B0042802molecular_functionidentical protein binding
B0061522molecular_function1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0009239biological_processenterobactin biosynthetic process
C0016289molecular_functionacyl-CoA hydrolase activity
C0016787molecular_functionhydrolase activity
C0016788molecular_functionhydrolase activity, acting on ester bonds
C0016790molecular_functionthiolester hydrolase activity
C0042802molecular_functionidentical protein binding
C0061522molecular_function1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0009239biological_processenterobactin biosynthetic process
D0016289molecular_functionacyl-CoA hydrolase activity
D0016787molecular_functionhydrolase activity
D0016788molecular_functionhydrolase activity, acting on ester bonds
D0016790molecular_functionthiolester hydrolase activity
D0042802molecular_functionidentical protein binding
D0061522molecular_function1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE 0FQ A 201
ChainResidue
AGLN48
AARG91
APRO92
AHOH303
AHOH393
BHIS106
BGLY108
BARG109
BGLN110
BASN111
DGLU63
APRO49
DSER67
DMET68
DGLY82
DTHR83
ALEU53
AHIS54
AGLY55
AASP76
AGLY77
AHIS89
AHIS90

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE 0FQ B 201
ChainResidue
AHIS106
AGLY108
AARG109
AGLN110
AASN111
BGLN48
BPRO49
BPHE50
BLEU53
BHIS54
BGLY55
BGLY77
BHIS89
BHIS90
BARG91
BPRO92
BHOH304
CGLU63
CSER67
CMET68
CVAL81
CGLY82

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 0FQ C 201
ChainResidue
BGLU63
BSER67
BMET68
BVAL81
BGLY82
BTHR83
CGLN48
CPRO49
CLEU53
CHIS54
CGLY55
CHIS89
CHIS90
CARG91
CPRO92
CHOH306
CHOH358
DGLY108
DARG109
DGLN110
DASN111

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE 0FQ D 201
ChainResidue
AGLU63
ASER67
AMET68
AGLY82
ATHR83
ALEU136
CHIS106
CGLY108
CARG109
CGLN110
CASN111
DGLN48
DPRO49
DLEU53
DHIS54
DGLY55
DARG75
DHIS89
DHIS90
DARG91
DPRO92
DHOH313

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile or proton acceptor => ECO:0000255|HAMAP-Rule:MF_00907, ECO:0000303|PubMed:25010423, ECO:0000305|PubMed:19193103
ChainResidueDetails
AGLU63
BGLU63
CGLU63
DGLU63

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:25010423
ChainResidueDetails
AGLN48
CHIS54
CGLY82
CHIS89
DGLN48
DHIS54
DGLY82
DHIS89
AHIS54
AGLY82
AHIS89
BGLN48
BHIS54
BGLY82
BHIS89
CGLN48

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PDB entries from 2024-07-24

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