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PDBsum entry 7txh
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173 a.a.
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496 a.a.
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292 a.a.
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PDB id:
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Hydrolase
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Title:
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Human mras q71r in complex with human shoc2 lrr domain m173i and human pp1ca
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Structure:
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Ras-related protein m-ras. Chain: a, d. Synonym: ras-related protein r-ras3. Engineered: yes. Mutation: yes. Leucine-rich repeat protein shoc-2. Chain: b, e. Synonym: protein soc-2 homolog,protein sur-8 homolog. Engineered: yes.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: mras, rras3. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: shoc2, kiaa0862. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.
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Resolution:
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1.95Å
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R-factor:
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0.169
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R-free:
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0.210
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Authors:
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Z.J.Hauseman,J.Viscomi,A.Dhembi,K.Clark,D.A.King,M.Fodor
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Key ref:
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Z.J.Hauseman
et al.
Cooperative assembly and structure of the ras-Shoc2-P holophosphatase provides insights into the ras signal and disease-Relevant mutations.
To be published,
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PubMed id:
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Date:
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09-Feb-22
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Release date:
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22-Jun-22
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PROCHECK
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Headers
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References
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O14807
(RASM_HUMAN) -
Ras-related protein M-Ras from Homo sapiens
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Seq: Struc:
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208 a.a.
173 a.a.*
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Enzyme class 1:
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Chains A, D:
E.C.3.6.5.2
- small monomeric GTPase.
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Reaction:
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GTP + H2O = GDP + phosphate + H+
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GTP
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H2O
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=
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GDP
Bound ligand (Het Group name = )
matches with 81.82% similarity
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phosphate
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+
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H(+)
Bound ligand (Het Group name = )
corresponds exactly
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Enzyme class 2:
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Chains C, F:
E.C.3.1.3.16
- protein-serine/threonine phosphatase.
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Reaction:
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1.
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O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate
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2.
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O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + phosphate
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O-phospho-L-seryl-[protein]
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+
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H2O
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=
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L-seryl-[protein]
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+
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phosphate
Bound ligand (Het Group name = )
corresponds exactly
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O-phospho-L-threonyl-[protein]
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+
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H2O
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=
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L-threonyl-[protein]
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+
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phosphate
Bound ligand (Het Group name = )
corresponds exactly
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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