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

2DBQ

Crystal Structure of Glyoxylate Reductase (PH0597) from Pyrococcus horikoshii OT3, Complexed with NADP (I41)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0016618molecular_functionhydroxypyruvate reductase [NAD(P)H] activity
A0030267molecular_functionglyoxylate reductase (NADPH) activity
A0047964molecular_functionglyoxylate reductase (NADH) activity
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 601
ChainResidue
ALYS41
ATYR78
AASN95
AARG160
AHOH612
AHOH641
AHOH673

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 602
ChainResidue
AVAL76
AGLY77
ALEU100
AARG241
AHIS288
ANAP401
AGOL501
AHOH646
ALEU53
AALA75

site_idAC3
Number of Residues37
DetailsBINDING SITE FOR RESIDUE NAP A 401
ChainResidue
ALYS42
AVAL76
ATHR104
AGLY157
ALEU158
AGLY159
AARG160
AILE161
ASER180
AARG181
ATHR182
AALA211
AVAL212
APRO213
ATHR218
AILE239
AALA240
AARG241
AASP265
AVAL266
AHIS288
AGLY290
ASER291
ASO4602
AHOH603
AHOH604
AHOH605
AHOH611
AHOH612
AHOH644
AHOH646
AHOH648
AHOH651
AHOH667
AHOH682
AHOH795
AHOH814

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 501
ChainResidue
AMSE52
ALEU53
ATYR74
AALA75
ATRP138
AHIS288
AMSE300
ASO4602
AHOH828

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
APRO35
AARG36
AGLU37
AGLU324
AHOH830

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 503
ChainResidue
ALYS243
APHE267
AGLU268
AGLU269
AGLU270
AHOH630
AHOH658
AHOH694
AHOH723

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 504
ChainResidue
ALYS151
AASP206
AHOH619
AHOH631
AHOH759

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 505
ChainResidue
APHE125
AARG134
APHE143
AHOH657
AHOH829
AHOH964

Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues28
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. IGIIGlGRIGqaiakrakgfnmr.ILyYS
ChainResidueDetails
AILE153-SER180

site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKkTaILINiARGkVVD
ChainResidueDetails
AMSE230-ASP246

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AARG241
AGLU270

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AHIS288

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|Ref.2
ChainResidueDetails
ALEU158
ASER180
AILE239
AHIS288

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1gdh
ChainResidueDetails
ALYS243
AASP265
AARG241
AGLU270
AHIS288

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gdh
ChainResidueDetails
AGLU270
AHIS288

225946

PDB entries from 2024-10-09

PDB statisticsPDBj update infoContact PDBjnumon