7nbh

Crystal structure of human serine racemase in complex with DSiP fragment Z26781964, XChem fragment screen.

spinqualitylabelsall models 7nbh, resolution 1.77Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7nbh is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.77Å Ligands: CA, CL, EDO, GOL, LLP, MG, NA, PGE, W0D Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SRR_HUMAN Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine. Publication Abstract from PubMed Human serine racemase (hSR) catalyses racemisation of L-serine to D-serine, the latter of which is a co-agonist of the NMDA subtype of glutamate receptors that are important in synaptic plasticity, learning and memory. In a 'closed' hSR structure containing the allosteric activator ATP, the inhibitor malonate is enclosed between the large and small domains while ATP is distal to the active site, residing at the dimer interface with the Tyr121 hydroxyl group contacting the alpha-phosphate of ATP. In contrast, in 'open' hSR structures, Tyr121 sits in the core of the small domain with its hydroxyl contacting the key catalytic residue Ser84. The ability to regulate SR activity by flipping Tyr121 from the core of the small domain to the dimer interface appears to have evolved in animals with a CNS. Multiple X-ray crystallographic enzyme-fragment structures show Tyr121 flipped out of its pocket in the core of the small domain. Data suggest that this ligandable pocket could be targeted by molecules that inhibit enzyme activity. Tyrosine 121 moves revealing a ligandable pocket that couples catalysis to ATP-binding in serine racemase.,Koulouris CR, Gardiner SE, Harris TK, Elvers KT, Mark Roe S, Gillespie JA, Ward SE, Grubisha O, Nicholls RA, Atack JR, Bax BD Commun Biol. 2022 Apr 11;5(1):346. doi: 10.1038/s42003-022-03264-5. PMID:35410329 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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