Crystal structure of human orotidine 5'-monophosphate decarboxylase complexed with 5-fluoro-UMP(produced from 5-fluoro-6-amino-UMP)
Liu, Y., Kotra, L.P., Pai, E.F.To be published.
Experimental Data Snapshot
Starting Model: experimental
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Entity ID: 1 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
Uridine 5'-monophosphate synthase | 312 | Homo sapiens | Mutation(s): 0  Gene Names: gi|13960142, OK/SW-cl.21, UMPS EC: 4.1.1.23 (PDB Primary Data), 2.4.2.10 (UniProt) | ||
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P11172 (Homo sapiens) Explore P11172  Go to UniProtKB:  P11172 | |||||
PHAROS:  P11172 GTEx:  ENSG00000114491  | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P11172 | ||||
Sequence AnnotationsExpand | |||||
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Ligands 1 Unique | |||||
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ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
5FU Query on 5FU | C [auth A], D [auth B] | 5-FLUORO-URIDINE-5'-MONOPHOSPHATE C9 H12 F N2 O9 P RNBMPPYRHNWTMA-UAKXSSHOSA-N |
Length ( Å ) | Angle ( ˚ ) |
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a = 70.29 | α = 90 |
b = 61.742 | β = 111.64 |
c = 71.212 | γ = 90 |
Software Name | Purpose |
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HKL-2000 | data collection |
MOLREP | phasing |
REFMAC | refinement |
Coot | model building |
HKL-2000 | data reduction |
HKL-2000 | data scaling |