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1SNN

3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0008686molecular_function3,4-dihydroxy-2-butanone-4-phosphate synthase activity
A0009231biological_processriboflavin biosynthetic process
A0016829molecular_functionlyase activity
A0030145molecular_functionmanganese ion binding
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0005829cellular_componentcytosol
B0008686molecular_function3,4-dihydroxy-2-butanone-4-phosphate synthase activity
B0009231biological_processriboflavin biosynthetic process
B0016829molecular_functionlyase activity
B0030145molecular_functionmanganese ion binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 5RP A 401
ChainResidue
AARG25
ATHR165
AILE183
AGLU185
AZN402
ACA403
AHOH623
AHOH668
AHOH746
AHOH750
AHOH751
AGLU26
AASP30
ACYS55
ATYR95
APHE101
AARG161
AGLY163
AHIS164

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 5RP B 501
ChainResidue
BARG25
BGLU26
BASP30
BCYS55
BPHE101
BARG161
BGLY163
BHIS164
BTHR165
BGLU185
BZN502
BCA503
BHOH632
BHOH664
BHOH672
BHOH679
BHOH686
BHOH705
BHOH706
BHOH707

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 402
ChainResidue
AGLU26
AHIS164
A5RP401
AHOH751

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AGLU26
ATYR95
A5RP401
AHOH668
AHOH750

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 502
ChainResidue
BGLU26
BHIS164
B5RP501
BHOH706

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 503
ChainResidue
BGLU26
B5RP501
BHOH664
BHOH705
BHOH707

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 601
ChainResidue
AASP96
AGLU97
AHOH654
AHOH671
AHOH676
AHOH706

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 602
ChainResidue
AGLU204
AASN207
AHOH688
BHOH514
BHOH554

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ZN A 603
ChainResidue
AHIS206

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:12904291, ECO:0000269|PubMed:15213409, ECO:0007744|PDB:1PVY, ECO:0007744|PDB:1SNN
ChainResidueDetails
AARG25
AASP30
AARG161
BARG25
BASP30
BARG161

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:12904291, ECO:0000305|PubMed:15213409, ECO:0007744|PDB:1PVY, ECO:0007744|PDB:1SNN
ChainResidueDetails
AGLU26
AHIS164
BGLU26
BHIS164

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Essential for catalytic activity
ChainResidueDetails
ASER147
AGLU185
BSER147
BGLU185

Catalytic Information from CSA
site_idCSA1
Number of Residues6
Detailsa catalytic site defined by CSA, PubMed 11827524, 12904291, 12200440
ChainResidueDetails
AGLU185
AASN106
ATYR95
AASP30
ASER147
ACYS55

site_idCSA2
Number of Residues6
Detailsa catalytic site defined by CSA, PubMed 11827524, 12904291, 12200440
ChainResidueDetails
BGLU185
BASN106
BTYR95
BASP30
BSER147
BCYS55

site_idMCSA1
Number of Residues6
DetailsM-CSA 648
ChainResidueDetails
AASP30proton shuttle (general acid/base)
ACYS55proton shuttle (general acid/base)
ATYR95electrostatic stabiliser
AASN106electrostatic stabiliser
ASER147electrostatic stabiliser, proton shuttle (general acid/base)
AGLU185proton shuttle (general acid/base)

site_idMCSA2
Number of Residues6
DetailsM-CSA 648
ChainResidueDetails
BASP30proton shuttle (general acid/base)
BCYS55proton shuttle (general acid/base)
BTYR95electrostatic stabiliser
BASN106electrostatic stabiliser
BSER147electrostatic stabiliser, proton shuttle (general acid/base)
BGLU185proton shuttle (general acid/base)

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PDB entries from 2024-08-21

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