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3RK8

Crystal structure of the chloride inhibited dihydrodipicolinate synthase from Acinetobacter baumannii complexed with pyruvate at 1.8 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008840molecular_function4-hydroxy-tetrahydrodipicolinate synthase activity
A0009085biological_processlysine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0016829molecular_functionlyase activity
A0019877biological_processdiaminopimelate biosynthetic process
A0044281biological_processsmall molecule metabolic process
A0046872molecular_functionmetal ion binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008840molecular_function4-hydroxy-tetrahydrodipicolinate synthase activity
B0009085biological_processlysine biosynthetic process
B0009089biological_processlysine biosynthetic process via diaminopimelate
B0016829molecular_functionlyase activity
B0019877biological_processdiaminopimelate biosynthetic process
B0044281biological_processsmall molecule metabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PYR A 292
ChainResidue
ATYR133
AHOH594
AVAL135
AARG138
ALYS161
AGLY186
AVAL205
AASN248
AHOH415
AHOH419

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 293
ChainResidue
ALYS15
ATHR264
AGLY265
AILE266
APRO272

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 294
ChainResidue
AGLN3
AGLY4
AASN37
AALA219
AILE222
AHOH352
AHOH447

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 295
ChainResidue
AASP20
ATRP21
ALYS22
AHOH424
AHOH438

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 296
ChainResidue
AGLU54
AGLU55
AGLN58
AHOH436

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 297
ChainResidue
AGLU25
AARG65
AHOH420

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 298
ChainResidue
AASP16
AARG267
AHOH404
AHOH443
AHOH445

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 299
ChainResidue
ATHR44
ALEU101
ALYS161
AHOH403
AHOH417

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PYR B 292
ChainResidue
BTYR133
BVAL135
BARG138
BLYS161
BGLY186
BVAL205
BASN248
BHOH425
BHOH428
BHOH605

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 293
ChainResidue
BLYS15
BTHR264
BGLY265
BILE266
BPRO272

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 294
ChainResidue
BALA182
BASP200
BGOL295
BHOH377
BHOH387
BHOH576

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 295
ChainResidue
BMET195
BGLY198
BALA199
BILE222
BLYS224
BGOL294
BHOH576
BHOH578

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 296
ChainResidue
BGLY165
BASP187
BGLU189
BHOH474
BHOH557
BHOH590

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG B 297
ChainResidue
BTRP21
BGLN58

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 298
ChainResidue
BLEU101
BLYS161
BHOH401
BHOH427
BHOH599

Functional Information from PROSITE/UniProt
site_idPS00665
Number of Residues18
DetailsDHDPS_1 Dihydrodipicolinate synthase signature 1. SIVavGTTGEAstlsmeE
ChainResidueDetails
ASER38-GLU55

site_idPS00666
Number of Residues31
DetailsDHDPS_2 Dihydrodipicolinate synthase signature 2. YNVPgrTgvdLsndtavrlaeipn.IvGIKDA
ChainResidueDetails
ATYR133-ALA163

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PDB entries from 2024-11-06

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