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6P35

2.5 Angstrom structure of wild type Glyoxylate/Hydroxypyruvate reductase A from Escherichia Coli in complex with 2-keto arginine and NADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008465molecular_functionhydroxypyruvate reductase (NADH) activity
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
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue NWG A 401
ChainResidue
AHIS46
AGLY64
AALA65
AGLY66
AARG227
AHIS275
ANAP405

site_idAC2
Number of Residues3
Detailsbinding site for residue GOL A 402
ChainResidue
APHE178
AGLN176
ASER177

site_idAC3
Number of Residues2
Detailsbinding site for residue GOL A 403
ChainResidue
AASP11
ANWG404

site_idAC4
Number of Residues8
Detailsbinding site for residue NWG A 404
ChainResidue
APHE10
AASP11
ATRP15
AGLU131
ATHR280
APRO282
AGOL403
AHOH541

site_idAC5
Number of Residues34
Detailsbinding site for residue NAP A 405
ChainResidue
AALA65
AARG89
AMET99
AGLY143
AALA144
AGLY145
AVAL146
ALEU147
ATRP165
ASER166
AARG167
ATHR168
ALYS170
ALEU197
ALEU198
APRO199
ALEU225
AALA226
AARG227
AASP251
AHIS275
AALA277
AALA278
ATYR312
ANWG401
AHOH504
AHOH524
AHOH529
AHOH539
AHOH543
AHOH580
AHOH583
AHOH600
AHOH607

site_idAC6
Number of Residues6
Detailsbinding site for residue SO4 A 406
ChainResidue
AHIS133
AARG134
AARG159
AARG281
AHOH511
AHOH520

site_idAC7
Number of Residues3
Detailsbinding site for residue SO4 A 407
ChainResidue
APRO48
AVAL49
ALYS73

site_idAC8
Number of Residues3
Detailsbinding site for residue SO4 A 408
ChainResidue
AARG113
APRO130
AHOH574

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

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PDB entries from 2024-07-17

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