Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3DDN

Crystal structure of hydroxypyruvic acid phosphate bound D-3-phosphoglycerate dehydrogenase in mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004617molecular_functionphosphoglycerate dehydrogenase activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006564biological_processL-serine biosynthetic process
A0009274cellular_componentpeptidoglycan-based cell wall
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0051287molecular_functionNAD binding
B0004617molecular_functionphosphoglycerate dehydrogenase activity
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0006564biological_processL-serine biosynthetic process
B0009274cellular_componentpeptidoglycan-based cell wall
B0016491molecular_functionoxidoreductase activity
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TLA A 530
ChainResidue
AARG446
AHIS447
AHOH788
BLYS439
BASP449
BLEU450
BARG451
BARG501

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TLA B 530
ChainResidue
AASP449
ALEU450
AARG451
AALA484
AARG501
BARG446
BHIS447
BSER488
BGLU489
ALYS439

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE TLA B 531
ChainResidue
BGLU361
BGLU363
BLYS402

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE HPV B 600
ChainResidue
AARG132
BSER52
BARG72
BGLY76
BASN99
BALA283
BGLN289
BHOH730

Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues28
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. VGVVGlGRIGqlvaqriaafgay.VVaYD
ChainResidueDetails
AVAL145-ASP172

site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LLarADFIsVHlPktpeTagLiD
ChainResidueDetails
ALEU193-ASP215

site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. TKpGvIIVNaARGgLVD
ChainResidueDetails
ATHR222-ASP238

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AARG233
AGLU262
BARG233
BGLU262

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AHIS280
BHIS280

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0A9T0
ChainResidueDetails
AARG152
BHIS280
AASP172
AALA231
AASP257
AHIS280
BARG152
BASP172
BALA231
BASP257

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1gdh
ChainResidueDetails
AHIS280
AASP257
AGLU262
AARG233
AGLY235

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1gdh
ChainResidueDetails
BHIS280
BASP257
BGLU262
BARG233
BGLY235

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gdh
ChainResidueDetails
AHIS280
AGLU262

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gdh
ChainResidueDetails
BHIS280
BGLU262

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon