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3C1N

Crystal Structure of Allosteric Inhibition Threonine-sensitive Aspartokinase from Methanococcus jannaschii with L-threonine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004072molecular_functionaspartate kinase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
A0009088biological_processthreonine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0009090biological_processhomoserine biosynthetic process
A0016301molecular_functionkinase activity
B0003824molecular_functioncatalytic activity
B0004072molecular_functionaspartate kinase activity
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0008652biological_processamino acid biosynthetic process
B0009088biological_processthreonine biosynthetic process
B0009089biological_processlysine biosynthetic process via diaminopimelate
B0009090biological_processhomoserine biosynthetic process
B0016301molecular_functionkinase activity
C0003824molecular_functioncatalytic activity
C0004072molecular_functionaspartate kinase activity
C0005524molecular_functionATP binding
C0005829cellular_componentcytosol
C0008652biological_processamino acid biosynthetic process
C0009088biological_processthreonine biosynthetic process
C0009089biological_processlysine biosynthetic process via diaminopimelate
C0009090biological_processhomoserine biosynthetic process
C0016301molecular_functionkinase activity
D0003824molecular_functioncatalytic activity
D0004072molecular_functionaspartate kinase activity
D0005524molecular_functionATP binding
D0005829cellular_componentcytosol
D0008652biological_processamino acid biosynthetic process
D0009088biological_processthreonine biosynthetic process
D0009089biological_processlysine biosynthetic process via diaminopimelate
D0009090biological_processhomoserine biosynthetic process
D0016301molecular_functionkinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE THR B 470
ChainResidue
AASN434
AILE435
BMET414
BALA417
BLYS418
BILE420
BALA421
BGLN440
BGLU444

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE THR A 471
ChainResidue
AMET414
AALA417
AGLY419
AILE420
AALA421
AGLN440
AGLU444
BASN434
BILE435

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE THR D 472
ChainResidue
CASN434
CILE435
DMET414
DALA417
DLYS418
DILE420
DALA421
DGLN440
DGLU444

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE THR A 473
ChainResidue
ALYS6
AGLY8
AGLY9
ATHR10
ASER11
ATRP229
ATHR230
AASP231

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE THR B 474
ChainResidue
BLYS6
BGLY8
BGLY9
BTHR10
BSER11
BTRP229
BTHR230
BASP231

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE THR C 475
ChainResidue
CGLY8
CTHR10
CSER11
CTRP229
CTHR230
CASP231
CLYS266

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE THR D 476
ChainResidue
DLYS6
DGLY8
DGLY9
DTHR10
DSER11
DTRP229
DTHR230
DASP231

Functional Information from PROSITE/UniProt
site_idPS00324
Number of Residues9
DetailsASPARTOKINASE Aspartokinase signature. VmKFGGTSV
ChainResidueDetails
AVAL4-VAL12

223532

PDB entries from 2024-08-07

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