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1O68

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 Residues6
DetailsBINDING SITE FOR RESIDUE NA A 274
ChainResidue
AASP43
AASP82
ALYS111
AKIV275
AHOH327
AHOH341

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA D 274
ChainResidue
DKIV275
DHOH311
DHOH312
DHOH375
DASP43
DASP82
DLYS111

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 274
ChainResidue
BASP43
BASP82
BLYS111
BKIV275
BHOH314
BHOH389

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA E 274
ChainResidue
EASP43
EASP82
ELYS111
EKIV275
EHOH345

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE KIV A 275
ChainResidue
ATHR21
ALEU40
AGLY42
AASP43
ASER44
AASP82
ALYS111
AHIS135
AGLU179
ANA274

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE KIV D 275
ChainResidue
DTHR21
DLEU40
DGLY42
DASP43
DSER44
DASP82
DLYS111
DILE200
DNA274
DHOH375

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE KIV B 275
ChainResidue
BTHR21
BLEU40
BGLY42
BASP43
BSER44
BASP82
BLYS111
BVAL210
BVAL212
BNA274

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE KIV E 275
ChainResidue
ETHR21
ELEU40
EGLY42
EASP43
ESER44
EASP82
ELYS111
EILE200
ENA274

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
DASP43
DASP82
DGLU113
EASP43
EASP82
EGLU113
AASP82
AGLU113
BASP43
BASP82
BGLU113
CASP43
CASP82
CGLU113

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

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PDB entries from 2024-10-30

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