Structure of PDB 4z0p Chain A

Receptor sequence

>4z0pA (length=316) Species: 266834 (Sinorhizobium meliloti 1021)

KSPVIVDLKFIPEEVEAALAGAFPGREVIDLADPAHQERDLSGIDYAVVW
KSAPDLFSRAPDLKVVFSGGAGVDHVLTLPGLPDVPLVRFVDRTLTTRMS
EWVMMQCLLHLRQHRAYEALAKKHEWRDLSQPEAADVTVGIMGMGVLGQD
AARKLAAMGFKVIGWSRSKRVIEGVETYDAAGLDAFLGRTDFLVGLLPLT
PDTRGIFNAALFAKLSRNGPFGAPVFINAGRGGSQVEADILECLDSGVLG
GASLDVFEREPLSPESRFWDMPNVYVTPHVAASSDVRALFVHVEHQIARF
ESGLPLEHVVDKVAGY

3D structure

• PDB: 4z0p Structural, Biochemical, and Evolutionary Characterizations of Glyoxylate/Hydroxypyruvate Reductases Show Their Division into Two Distinct Subfamilies.
• Chain: A
• Resolution: 1.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): L98 R234 G253 D258 E263 H282
• Catalytic site (residue number reindexed from 1): L95 R231 G250 D255 E260 H279
• Enzyme Commision number: 1.1.1.79: glyoxylate reductase (NADP(+)).

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	OXD	A	W53 G73 A74 G75 R234 H282	W50 G70 A71 G72 R231 H279
BS02	OXD	A	H117 R118	H114 R115
BS03	NDP	A	R92 M102 M147 G148 V149 L150 W168 S169 R170 S171 R173 L200 P201 A232 G233 R234 H282 A284 A285 Y319	R89 M99 M144 G145 V146 L147 W165 S166 R167 S168 R170 L197 P198 A229 G230 R231 H279 A281 A282 Y316

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0051287 NAD binding

External links

• PDB: RCSB:4z0p, PDBe:4z0p, PDBj:4z0p
• PDBsum: 4z0p
• PubMed: 29309127
• UniProt: Q92T34