Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2WWR

Crystal Structure of Human Glyoxylate Reductase Hydroxypyruvate Reductase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005782	cellular_component	peroxisomal matrix
A	0005829	cellular_component	cytosol
A	0008465	molecular_function	hydroxypyruvate reductase (NADH) activity
A	0016491	molecular_function	oxidoreductase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0016618	molecular_function	hydroxypyruvate reductase [NAD(P)H] activity
A	0019752	biological_process	carboxylic acid metabolic process
A	0030267	molecular_function	glyoxylate reductase (NADPH) activity
A	0031406	molecular_function	carboxylic acid binding
A	0042803	molecular_function	protein homodimerization activity
A	0043648	biological_process	dicarboxylic acid metabolic process
A	0046487	biological_process	glyoxylate metabolic process
A	0050661	molecular_function	NADP binding
A	0051287	molecular_function	NAD binding
A	0070062	cellular_component	extracellular exosome
A	0070402	molecular_function	NADPH binding
A	1902494	cellular_component	catalytic complex
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005782	cellular_component	peroxisomal matrix
B	0005829	cellular_component	cytosol
B	0008465	molecular_function	hydroxypyruvate reductase (NADH) activity
B	0016491	molecular_function	oxidoreductase activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0016618	molecular_function	hydroxypyruvate reductase [NAD(P)H] activity
B	0019752	biological_process	carboxylic acid metabolic process
B	0030267	molecular_function	glyoxylate reductase (NADPH) activity
B	0031406	molecular_function	carboxylic acid binding
B	0042803	molecular_function	protein homodimerization activity
B	0043648	biological_process	dicarboxylic acid metabolic process
B	0046487	biological_process	glyoxylate metabolic process
B	0050661	molecular_function	NADP binding
B	0051287	molecular_function	NAD binding
B	0070062	cellular_component	extracellular exosome
B	0070402	molecular_function	NADPH binding
B	1902494	cellular_component	catalytic complex
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005782	cellular_component	peroxisomal matrix
C	0005829	cellular_component	cytosol
C	0008465	molecular_function	hydroxypyruvate reductase (NADH) activity
C	0016491	molecular_function	oxidoreductase activity
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0016618	molecular_function	hydroxypyruvate reductase [NAD(P)H] activity
C	0019752	biological_process	carboxylic acid metabolic process
C	0030267	molecular_function	glyoxylate reductase (NADPH) activity
C	0031406	molecular_function	carboxylic acid binding
C	0042803	molecular_function	protein homodimerization activity
C	0043648	biological_process	dicarboxylic acid metabolic process
C	0046487	biological_process	glyoxylate metabolic process
C	0050661	molecular_function	NADP binding
C	0051287	molecular_function	NAD binding
C	0070062	cellular_component	extracellular exosome
C	0070402	molecular_function	NADPH binding
C	1902494	cellular_component	catalytic complex
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005782	cellular_component	peroxisomal matrix
D	0005829	cellular_component	cytosol
D	0008465	molecular_function	hydroxypyruvate reductase (NADH) activity
D	0016491	molecular_function	oxidoreductase activity
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0016618	molecular_function	hydroxypyruvate reductase [NAD(P)H] activity
D	0019752	biological_process	carboxylic acid metabolic process
D	0030267	molecular_function	glyoxylate reductase (NADPH) activity
D	0031406	molecular_function	carboxylic acid binding
D	0042803	molecular_function	protein homodimerization activity
D	0043648	biological_process	dicarboxylic acid metabolic process
D	0046487	biological_process	glyoxylate metabolic process
D	0050661	molecular_function	NADP binding
D	0051287	molecular_function	NAD binding
D	0070062	cellular_component	extracellular exosome
D	0070402	molecular_function	NADPH binding
D	1902494	cellular_component	catalytic complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG B 1328

Chain	Residue
B	ASP253

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG D 1328

Chain	Residue
A	ASP37
D	ASP253

Functional Information from PROSITE/UniProt

site_id	PS00671
Number of Residues	17
Details	D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKeTaVFINiSRGdVVN

Chain	Residue	Details
A	MET234-ASN250

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000305\|PubMed:16756993

Chain	Residue	Details
A	HIS293
B	HIS293
C	HIS293
D	HIS293

site_id	SWS_FT_FI2
Number of Residues	36
Details	BINDING: BINDING => ECO:0000269\|PubMed:16756993

Chain	Residue	Details
A	VAL83
B	VAL83
B	GLY162
B	ARG185
B	SER217
B	ILE243
B	ARG245
B	ASP269
B	HIS293
B	GLY295
C	VAL83
A	GLY162
C	GLY162
C	ARG185
C	SER217
C	ILE243
C	ARG245
C	ASP269
C	HIS293
C	GLY295
D	VAL83
D	GLY162
A	ARG185
D	ARG185
D	SER217
D	ILE243
D	ARG245
D	ASP269
D	HIS293
D	GLY295
A	SER217
A	ILE243
A	ARG245
A	ASP269
A	HIS293
A	GLY295

site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Raises pKa of active site His => ECO:0000305\|PubMed:16756993

Chain	Residue	Details
A	GLU274
B	GLU274
C	GLU274
D	GLU274

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER36
A	SER272
B	SER36
B	SER272
C	SER36
C	SER272
D	SER36
D	SER272

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	THR298
B	THR298
C	THR298
D	THR298

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)