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PDBsum entry 5e95

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protein ligands metals Protein-protein interface(s) links
Signaling protein/inhibitor PDB id
5e95

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
92 a.a.
168 a.a.
Ligands
GDP
Metals
_MG
Waters ×372
PDB id:
5e95
Name: Signaling protein/inhibitor
Title: Crystal structure of mb(ns1)/h-ras complex
Structure: Mb(ns1). Chain: b. Engineered: yes. Gtpase hras. Chain: a. Fragment: unp residues 1-166. Synonym: h-ras-1,ha-ras,transforming protein p21,c-h-ras,p21ras. Engineered: yes
Source: Homo sapiens. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Human. Gene: hras, hras1.
Resolution:
1.40Å     R-factor:   0.164     R-free:   0.192
Authors: R.R.Eguchi,F.Sha,A.Gupta,A.Koide,S.Koide
Key ref: R.Spencer-Smith et al. (2017). Inhibition of RAS function through targeting an allosteric regulatory site. Nat Chem Biol, 13, 62-68. PubMed id: 27820802 DOI: 10.1038/nchembio.2231
Date:
14-Oct-15     Release date:   02-Nov-16    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
No UniProt id for this chain
Struc: 92 a.a.
Protein chain
Pfam   ArchSchema ?
P01112  (RASH_HUMAN) -  GTPase HRas from Homo sapiens
Seq:
Struc:
189 a.a.
168 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chain A: E.C.3.6.5.2  - small monomeric GTPase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: GTP + H2O = GDP + phosphate + H+
GTP
+ H2O
=
GDP
Bound ligand (Het Group name = GDP)
corresponds exactly
+ phosphate
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1038/nchembio.2231 Nat Chem Biol 13:62-68 (2017)
PubMed id: 27820802  
 
 
Inhibition of RAS function through targeting an allosteric regulatory site.
R.Spencer-Smith, A.Koide, Y.Zhou, R.R.Eguchi, F.Sha, P.Gajwani, D.Santana, A.Gupta, M.Jacobs, E.Herrero-Garcia, J.Cobbert, H.Lavoie, M.Smith, T.Rajakulendran, E.Dowdell, M.N.Okur, I.Dementieva, F.Sicheri, M.Therrien, J.F.Hancock, M.Ikura, S.Koide, J.P.O'Bryan.
 
  ABSTRACT  
 
No abstract given.

 

 

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