7NBF
Crystal structure of human serine racemase in complex with DSiP fragment Z126932614, XChem fragment screen.
This is a non-PDB format compatible entry.
Summary for 7NBF
| Entry DOI | 10.2210/pdb7nbf/pdb |
| Related | 6ZSP 6ZUJ |
| Descriptor | Serine racemase, TRIETHYLENE GLYCOL, CHLORIDE ION, ... (12 entities in total) |
| Functional Keywords | racemase, xchem, inhibitor, isomerase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 153472.47 |
| Authors | Koulouris, C.R.,Roe, S.M. (deposition date: 2021-01-26, release date: 2021-03-03, Last modification date: 2024-01-31) |
| Primary citation | Koulouris, C.R.,Gardiner, S.E.,Harris, T.K.,Elvers, K.T.,Mark Roe, S.,Gillespie, J.A.,Ward, S.E.,Grubisha, O.,Nicholls, R.A.,Atack, J.R.,Bax, B.D. Tyrosine 121 moves revealing a ligandable pocket that couples catalysis to ATP-binding in serine racemase. Commun Biol, 5:346-346, 2022 Cited by PubMed Abstract: 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 α-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. PubMed: 35410329DOI: 10.1038/s42003-022-03264-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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