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7JQI

Structure of wild type Glyoxylate/Hydroxypyruvate reductase A from Escherichia Coli in complex with alpha-ketoglutarate and NADP+

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005737cellular_componentcytoplasm
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 Residues8
Detailsbinding site for residue AKG A 401
ChainResidue
ATRP45
AGLY64
AALA65
AGLY66
AARG227
AHIS275
AALA278
ANAP402

site_idAC2
Number of Residues34
Detailsbinding site for residue NAP A 402
ChainResidue
AARG89
AMET99
AGLY143
AALA144
AGLY145
AVAL146
ALEU147
ATRP165
ASER166
AARG167
ATHR168
ALYS170
ALEU197
ALEU198
APRO199
ALEU225
AALA226
AARG227
AASP251
AHIS275
AALA277
AALA278
ATYR312
AAKG401
AHOH520
AHOH544
AHOH546
AHOH563
AHOH581
AHOH588
AHOH590
AHOH609
AHOH634
AALA65

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

219869

PDB entries from 2024-05-15

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