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1O66

Crystal structure of 3-methyl-2-oxobutanoate hydroxymethyltransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0003864molecular_function3-methyl-2-oxobutanoate hydroxymethyltransferase activity
A0005737cellular_componentcytoplasm
A0015940biological_processpantothenate biosynthetic process
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0003864molecular_function3-methyl-2-oxobutanoate hydroxymethyltransferase activity
B0005737cellular_componentcytoplasm
B0015940biological_processpantothenate biosynthetic process
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0003824molecular_functioncatalytic activity
C0003864molecular_function3-methyl-2-oxobutanoate hydroxymethyltransferase activity
C0005737cellular_componentcytoplasm
C0015940biological_processpantothenate biosynthetic process
C0016740molecular_functiontransferase activity
C0046872molecular_functionmetal ion binding
D0000287molecular_functionmagnesium ion binding
D0003824molecular_functioncatalytic activity
D0003864molecular_function3-methyl-2-oxobutanoate hydroxymethyltransferase activity
D0005737cellular_componentcytoplasm
D0015940biological_processpantothenate biosynthetic process
D0016740molecular_functiontransferase activity
D0046872molecular_functionmetal ion binding
E0000287molecular_functionmagnesium ion binding
E0003824molecular_functioncatalytic activity
E0003864molecular_function3-methyl-2-oxobutanoate hydroxymethyltransferase activity
E0005737cellular_componentcytoplasm
E0015940biological_processpantothenate biosynthetic process
E0016740molecular_functiontransferase activity
E0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 274
ChainResidue
AARG61
AASP62
BARG61
BASP62
BGOL274

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 274
ChainResidue
DGOL274
CARG61
CASP62
DARG61
DASP62

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 274
ChainResidue
AARG61
AASP62
AGOL274
BARG61
BASP62

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL D 274
ChainResidue
CARG61
CASP62
CGOL274
DARG61
DASP62

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL E 274
ChainResidue
EARG61
EARG61
EASP62
EASP62
ETYR65

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00156
ChainResidueDetails
AGLU179
BGLU179
CGLU179
DGLU179
EGLU179

site_idSWS_FT_FI2
Number of Residues15
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00156
ChainResidueDetails
AASP43
AASP82
AGLU113
BASP43
BASP82
BGLU113
CASP43
CASP82
CGLU113
DASP43
DASP82
DGLU113
EASP43
EASP82
EGLU113

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING:
ChainResidueDetails
ALYS111
BLYS111
CLYS111
DLYS111
ELYS111

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PDB entries from 2024-05-01

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