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6OVL

2.1 Angstrom structure of wild type Glyoxylate/Hydroxypyruvate reductase A from Escherichia Coli in complex with glyoxylate and NADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008465molecular_functionglycerate dehydrogenase activity
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0016618molecular_functionhydroxypyruvate reductase activity
A0030267molecular_functionglyoxylate reductase (NADPH) activity
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue GOL A 401
ChainResidue
AGLU97
AGLN100
ASER154
ATHR157
AHOH503
AHOH665

site_idAC2
Number of Residues7
Detailsbinding site for residue PO4 A 402
ChainResidue
AARG281
AHOH508
AHOH521
AHOH611
AHIS133
AARG134
AARG159

site_idAC3
Number of Residues37
Detailsbinding site for residue NAP A 403
ChainResidue
AALA65
AARG89
AMET99
AALA144
AGLY145
AVAL146
ALEU147
ATRP165
ASER166
AARG167
ATHR168
ALYS170
ALEU197
ALEU198
APRO199
ATHR204
ALEU225
AALA226
AARG227
AASP251
AHIS275
AALA277
AALA278
ATYR312
AGLV404
APO4407
AHOH530
AHOH539
AHOH541
AHOH549
AHOH581
AHOH589
AHOH609
AHOH633
AHOH643
AHOH682
AHOH683

site_idAC4
Number of Residues7
Detailsbinding site for residue GLV A 404
ChainResidue
AGLY64
AALA65
AGLY66
AARG227
AHIS275
ANAP403
AHOH515

site_idAC5
Number of Residues3
Detailsbinding site for residue K A 405
ChainResidue
AGLU233
ASER262
AHOH639

site_idAC6
Number of Residues2
Detailsbinding site for residue NA A 406
ChainResidue
AGLN13
AARG20

site_idAC7
Number of Residues6
Detailsbinding site for residue PO4 A 407
ChainResidue
ATRP165
AARG167
AGLY180
AARG181
ANAP403
AHOH584

Functional Information from PROSITE/UniProt
site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. LPdGaYLLNlARGvHVV
ChainResidueDetails
ALEU216-VAL232

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AARG227

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AHIS275

221051

PDB entries from 2024-06-12

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