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PDBsum entry 3rj3

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protein ligands Protein-protein interface(s) links
Protein binding PDB id
3rj3

 

 

 

 

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Contents
Protein chains
292 a.a.
125 a.a.
107 a.a.
Ligands
GOL ×4
Waters ×372
PDB id:
3rj3
Name: Protein binding
Title: Complement components factor h ccp19-20 (s1191l mutant) and c3d in complex
Structure: Complement c3d fragment. Chain: a, b, c. Fragment: unp residues 996-1303. Synonym: c3d. Engineered: yes. Complement factor h-related protein 1. Chain: d, e, f. Fragment: unp residues 206-330. Synonym: fhr-1, h factor-like protein 1, h-factor-like 1, h36.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: c3, cpamd1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: cfhr1, cfhl, cfhl1, cfhl1p, cfhr1p, fhr1, hfl1, hfl2. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Resolution:
2.35Å     R-factor:   0.193     R-free:   0.232
Authors: H.P.Morgan,J.P.Hannan
Key ref: A.P.Herbert et al. (2012). Structural and functional characterization of the product of disease-related factor H gene conversion. Biochemistry, 51, 1874-1884. PubMed id: 22320225
Date:
15-Apr-11     Release date:   14-Mar-12    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P01024  (CO3_HUMAN) -  Complement C3 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1663 a.a.
292 a.a.*
Protein chains
Pfam   ArchSchema ?
P08603  (CFAH_HUMAN) -  Complement factor H from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1231 a.a.
125 a.a.*
Protein chain
Pfam   ArchSchema ?
P08603  (CFAH_HUMAN) -  Complement factor H from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1231 a.a.
107 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 

 
Biochemistry 51:1874-1884 (2012)
PubMed id: 22320225  
 
 
Structural and functional characterization of the product of disease-related factor H gene conversion.
A.P.Herbert, D.Kavanagh, C.Johansson, H.P.Morgan, B.S.Blaum, J.P.Hannan, P.N.Barlow, D.Uhrín.
 
  ABSTRACT  
 
No abstract given.

 

 

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