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2DBZ

Crystal Structure of Glyoxylate Reductase (PH0597) from Pyrococcus horikoshii OT3, Complexed with NADP (P61)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0047964molecular_functionglyoxylate reductase (NADH) activity
A0051287molecular_functionNAD binding
B0005737cellular_componentcytoplasm
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0047964molecular_functionglyoxylate reductase (NADH) activity
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 501
ChainResidue
BTYR78
BASN95
BARG160
BHOH530

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
ATYR78
AASN95
AARG160

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 503
ChainResidue
BVAL76
BGLY77
BARG241
BHIS288
BSER291
BNAP402
BLEU53
BALA75

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 504
ChainResidue
ALEU53
AALA75
AVAL76
AGLY77
ALEU100
AARG241
AHIS288
ASER291
ANAP401

site_idAC5
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAP A 401
ChainResidue
ALYS42
AVAL76
AGLY77
ATHR104
ALEU158
AGLY159
AARG160
AILE161
ASER180
AARG181
ATHR182
AALA211
APRO213
AGLU217
ATHR218
AILE239
AALA240
AARG241
AASP265
AHIS288
AGLY290
ASER291
ASO4504
AHOH512

site_idAC6
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NAP B 402
ChainResidue
BLYS42
BVAL76
BGLY77
BTHR104
BGLY157
BLEU158
BGLY159
BARG160
BILE161
BSER180
BARG181
BTHR182
BALA211
BVAL212
BPRO213
BGLU217
BTHR218
BILE239
BALA240
BARG241
BASP265
BHIS288
BGLY290
BSER291
BSO4503
BHOH510
BHOH530

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
AMET230-ASP246

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AARG241
AGLU270
BARG241
BGLU270

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AHIS288
BHIS288

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|Ref.2
ChainResidueDetails
ALEU158
ASER180
AILE239
AHIS288
BLEU158
BSER180
BILE239
BHIS288

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 Residues5
DetailsAnnotated By Reference To The Literature 1gdh
ChainResidueDetails
BLYS243
BASP265
BARG241
BGLU270
BHIS288

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gdh
ChainResidueDetails
AGLU270
AHIS288

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gdh
ChainResidueDetails
BGLU270
BHIS288

223166

PDB entries from 2024-07-31

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