Structure of PDB 5nzq Chain A

Receptor sequence
>5nzqA (length=195) Species: 9606 (Homo sapiens) [Search protein sequence]
NGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLG
ILGLGRIGREVATRMQSFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPL
CDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALLRAL
QSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSR
3D structure
PDB5nzq Validating and enabling phosphoglycerate dehydrogenase (PHGDH) as a target for fragment-based drug discovery in PHGDH-amplified breast cancer.
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N102 R236 D260 E265 H283
Catalytic site (residue number reindexed from 1) N3 R137 D161 E166 H184
Enzyme Commision number 1.1.1.37: malate dehydrogenase.
1.1.1.399: 2-oxoglutarate reductase.
1.1.1.95: phosphoglycerate dehydrogenase.
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 5AO A Y174 P176 T207 P208 Y75 P77 T108 P109 BindingDB: Kd=9300000nM
Gene Ontology
Molecular Function
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0051287 NAD binding

View graph for
Molecular Function
External links
PDB RCSB:5nzq, PDBe:5nzq, PDBj:5nzq
PDBsum5nzq
PubMed29568346
UniProtO43175|SERA_HUMAN D-3-phosphoglycerate dehydrogenase (Gene Name=PHGDH)

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