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3AAW

Crystal structure of aspartate kinase from Corynebacterium glutamicum in complex with lysine and threonine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004072molecular_functionaspartate kinase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
A0009085biological_processlysine biosynthetic process
A0009088biological_processthreonine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0009090biological_processhomoserine biosynthetic process
A0016301molecular_functionkinase activity
A0019877biological_processdiaminopimelate biosynthetic process
B0003824molecular_functioncatalytic activity
B0004072molecular_functionaspartate kinase activity
B0005829cellular_componentcytosol
B0009088biological_processthreonine biosynthetic process
B0009089biological_processlysine biosynthetic process via diaminopimelate
B0009090biological_processhomoserine biosynthetic process
B0016301molecular_functionkinase activity
C0004072molecular_functionaspartate kinase activity
C0005524molecular_functionATP binding
C0005829cellular_componentcytosol
C0008652biological_processamino acid biosynthetic process
C0009085biological_processlysine biosynthetic process
C0009088biological_processthreonine biosynthetic process
C0009089biological_processlysine biosynthetic process via diaminopimelate
C0009090biological_processhomoserine biosynthetic process
C0016301molecular_functionkinase activity
C0019877biological_processdiaminopimelate biosynthetic process
D0003824molecular_functioncatalytic activity
D0004072molecular_functionaspartate kinase activity
D0005829cellular_componentcytosol
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 Residues10
DetailsBINDING SITE FOR RESIDUE THR B 201
ChainResidue
AASN374
BHOH205
AILE375
BASP25
BLYS26
BGLY28
BGLU29
BALA30
BGLN49
BHOH204

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE THR A 501
ChainResidue
AASP274
ALYS275
AGLY277
AGLU278
AALA279
AGLN298
AHOH716
AHOH717
BASN125
BILE126

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE LYS A 601
ChainResidue
AMET354
ALYS355
AHIS357
AGLY359
AVAL360
ATHR361
ATHR380
ASER381
AHOH672
AHOH770
BASN43
BILE44
BASP45
BHOH195

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE THR D 201
ChainResidue
CASN374
CILE375
CHOH715
DASP25
DLYS26
DGLY28
DGLU29
DALA30
DGLN49
DHOH618

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE LYS C 601
ChainResidue
CMET354
CHIS357
CGLY359
CVAL360
CTHR361
CSER381
CGLU382
CHOH677
CHOH739
DASN43
DILE44
DASP45

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE THR C 501
ChainResidue
CASP274
CLYS275
CGLY277
CGLU278
CALA279
CGLN298
CTHR308
CHOH678
CHOH679
DASN125
DILE126

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE LYS C 701
ChainResidue
CLYS7
CGLY10
CSER41
CGLU74
CARG151
CGLY153
CSER154
CASP155

Functional Information from PROSITE/UniProt
site_idPS00324
Number of Residues9
DetailsASPARTOKINASE Aspartokinase signature. VqKYGGSSL
ChainResidueDetails
AVAL5-LEU13

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS7
AASP274
CLYS7
CARG25
CSER41
CGLU74
CLEU125
CARG151
CSER174
CTYR180
CLYS210
AARG25
CASP274
ASER41
AGLU74
ALEU125
AARG151
ASER174
ATYR180
ALYS210

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING:
ChainResidueDetails
AASP45
CASN292
CGLN298
CVAL360
CASN374
CSER381
ASER154
AASN292
AGLN298
AVAL360
AASN374
ASER381
CASP45
CSER154

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Contribution to the catalysis => ECO:0000250
ChainResidueDetails
ALYS7
AGLU74
CLYS7
CGLU74

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PDB entries from 2024-07-24

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