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PDBsum entry 3msx

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protein ligands metals Protein-protein interface(s) links
Protein binding PDB id
3msx

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
177 a.a.
192 a.a.
Ligands
GDP
MGF
Metals
_MG
Waters ×222
PDB id:
3msx
Name: Protein binding
Title: Crystal structure of rhoa.Gdp.Mgf3 in complex with gap domain of arhgap20
Structure: Transforming protein rhoa. Chain: a. Synonym: rho cdna clone 12, h12. Engineered: yes. Mutation: yes. Rho gtpase-activating protein 20. Chain: b. Fragment: gap domain. Synonym: rho-type gtpase-activating protein 20.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: arh12, arha, rho12, rhoa. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: arhgap20, kiaa1391.
Resolution:
1.65Å     R-factor:   0.196     R-free:   0.219
Authors: D.Utepbergenov,D.R.Cooper,U.Derewenda,Z.S.Derewenda
Key ref: D.Utepbergenov et al. Mechanism of molecular specificity of rhogap domains small gtpases of rhoa family.. To be published, .
Date:
29-Apr-10     Release date:   16-Mar-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P61586  (RHOA_HUMAN) -  Transforming protein RhoA from Homo sapiens
Seq:
Struc:
193 a.a.
177 a.a.*
Protein chain
Pfam   ArchSchema ?
Q9P2F6  (RHG20_HUMAN) -  Rho GTPase-activating protein 20 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1191 a.a.
192 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class 2: 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(+)
   Enzyme class 3: Chain B: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
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.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

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