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Crystal structure of phosphoglycerate dehydrogenase from Pyrococcus horikoshii OT3

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0051287molecular_functionNAD binding
B0000166molecular_functionnucleotide binding
B0016491molecular_functionoxidoreductase activity
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 Residues30
DetailsBINDING SITE FOR RESIDUE NAD A 1001
ChainResidue
AVAL100
ATYR171
AVAL201
APRO202
ASER206
ATHR207
ATHR228
ASER229
AARG230
AASP254
AHIS278
AGLY146
AGLY280
AALA281
AHOH1006
AHOH1007
AHOH1020
AHOH1024
AHOH1025
AHOH1041
AHOH1047
AHOH1076
APHE147
AHOH1113
AGLY148
AARG149
AILE150
ATYR168
AASP169
APRO170

site_idAC2
Number of Residues29
DetailsBINDING SITE FOR RESIDUE NAD B 2001
ChainResidue
BVAL100
BPHE147
BGLY148
BARG149
BILE150
BTYR168
BASP169
BPRO170
BTYR171
BHIS200
BVAL201
BPRO202
BSER206
BTHR207
BTHR228
BSER229
BASP254
BHIS278
BGLY280
BALA281
BHOH2008
BHOH2013
BHOH2035
BHOH2084
BHOH2097
BHOH2099
BHOH2113
BHOH2159
BHOH2218

Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues28
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. IGIIGfGRIGyqvakianalgmn.ILlYD
ChainResidueDetails
AILE142-ASP169

site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LLkeSDVVtIHvPlvesTyhLiN
ChainResidueDetails
ALEU190-ASN212

site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKkTaILINtSRGpVVD
ChainResidueDetails
AMET219-ASP235

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1psd
ChainResidueDetails
AGLU259
AHIS278

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1psd
ChainResidueDetails
BGLU259
BHIS278

226707

PDB entries from 2024-10-30

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