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1G58

CRYSTAL STRUCTURE OF 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE GOLD DERIVATIVE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0008686molecular_function3,4-dihydroxy-2-butanone-4-phosphate synthase activity
A0009231biological_processriboflavin biosynthetic process
A0016829molecular_functionlyase activity
A0030145molecular_functionmanganese ion binding
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0008686molecular_function3,4-dihydroxy-2-butanone-4-phosphate synthase activity
B0009231biological_processriboflavin biosynthetic process
B0016829molecular_functionlyase activity
B0030145molecular_functionmanganese ion binding
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE AU B 301
ChainResidue
BLEU5
BLEU57
BHOH355
BHOH362
BHOH449

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE AU A 302
ChainResidue
AHOH400
AGLY41
AARG184
AALA185
ACYS188

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00180
ChainResidueDetails
AARG37
BHIS153
AGLU38
AASP42
AARG150
AHIS153
BARG37
BGLU38
BASP42
BARG150

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Essential for catalytic activity
ChainResidueDetails
AHIS136
AGLU174
BHIS136
BGLU174

227344

PDB entries from 2024-11-13

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