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5V72

Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase SMc04462 (SmGhrB) from Sinorhizobium meliloti in complex with citrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
B0000166molecular_functionnucleotide binding
B0005829cellular_componentcytosol
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0016618molecular_functionhydroxypyruvate reductase [NAD(P)H] activity
B0030267molecular_functionglyoxylate reductase (NADPH) activity
B0046872molecular_functionmetal ion binding
B0051287molecular_functionNAD binding
C0000166molecular_functionnucleotide binding
C0005829cellular_componentcytosol
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0016618molecular_functionhydroxypyruvate reductase [NAD(P)H] activity
C0030267molecular_functionglyoxylate reductase (NADPH) activity
C0046872molecular_functionmetal ion binding
C0051287molecular_functionNAD binding
D0000166molecular_functionnucleotide binding
D0005829cellular_componentcytosol
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0016618molecular_functionhydroxypyruvate reductase [NAD(P)H] activity
D0030267molecular_functionglyoxylate reductase (NADPH) activity
D0046872molecular_functionmetal ion binding
D0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue NA A 401
ChainResidue
AALA191
AGLU192
AVAL194
AALA218
ALEU219
AHOH668

site_idAC2
Number of Residues4
Detailsbinding site for residue CL A 402
ChainResidue
AHOH776
AASN13
AARG286
AHOH774

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 403
ChainResidue
ALEU96
AGLY229
AHIS277
ASER280

site_idAC4
Number of Residues6
Detailsbinding site for residue NA B 401
ChainResidue
BALA191
BGLU192
BVAL194
BALA218
BLEU219
CHOH667

site_idAC5
Number of Residues3
Detailsbinding site for residue CL B 402
ChainResidue
BASN13
BARG286
BHOH699

site_idAC6
Number of Residues7
Detailsbinding site for residue NA C 401
ChainResidue
CALA191
CGLU192
CVAL194
CALA218
CLEU219
CHOH615
CHOH715

site_idAC7
Number of Residues4
Detailsbinding site for residue NA C 402
ChainResidue
CVAL228
CGLY229
CCIT403
CHOH638

site_idAC8
Number of Residues15
Detailsbinding site for residue CIT C 403
ChainResidue
CVAL72
CILE153
CVAL228
CGLY229
CHIS277
CALA279
CSER280
CNA402
CHOH501
CHOH529
CHOH562
CHOH582
CHOH584
CHOH634
CHOH638

site_idAC9
Number of Residues3
Detailsbinding site for residue CL C 404
ChainResidue
CASN13
CARG286
CHOH776

site_idAD1
Number of Residues6
Detailsbinding site for residue NA D 401
ChainResidue
DALA191
DGLU192
DVAL194
DALA218
DLEU219
DHOH647

site_idAD2
Number of Residues3
Detailsbinding site for residue CL D 402
ChainResidue
DASN13
DARG286
DHOH679

226707

PDB entries from 2024-10-30

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